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The S. pombe gene epe1+ (synonym jhd1) encodes Epe1, a nuclear heterochromatin-associated JmjC-family protein that is recruited to H3K9-methylated chromatin primarily through interaction with Swi6/HP1. Across multiple mechanistic studies, Epe1 emerges as a negative regulator (“anti-silencing factor”) of heterochromatin assembly and spreading, acting at heterochromatin boundaries and within heterochromatin to control domain stability and epigenetic variability. While Epe1 is annotated as a putative 2-oxoglutarate/Fe(II) dioxygenase/histone demethylase, direct in vitro H3K9 demethylase activity is repeatedly difficult to detect, and several influential studies propose that Epe1’s dominant in vivo functions are non-enzymatic, mediated by protein–protein interactions (especially with Swi6/HP1) that antagonize histone deacetylase activity. More recent work supports dual functions: an N-terminal transcriptional activation domain (NTA) can prevent de novo ectopic H3K9 methylation, whereas the JmjC module contributes to removal of established ectopic heterochromatin in vivo. Nutrient and stress signaling pathways regulate Epe1’s abundance and localization, linking environmental inputs to heterochromatin remodeling, epigenetic adaptation, and drug resistance phenotypes. (sorida2019regulationofectopic pages 1-2, isaac2007interactionofepe1 pages 1-2, raiymbek2020anh3k9methylationdependent pages 2-3, raiymbek2020anh3k9methylationdependent pages 20-22, yaseen2022proteasomedependenttruncationof pages 8-9, bao2022thecampsignaling pages 8-9, larkin2024mappingthedynamics pages 5-7)
The literature retrieved consistently refers to Epe1 (also called Jhd1 in S. pombe) as a JmjC-family heterochromatin regulator recruited by Swi6/HP1 and affecting heterochromatin domain integrity and spreading. This matches the UniProt-provided identity (O94603; SPCC622.16c) and is distinct from the better-known budding-yeast “Jhd1” that demethylates H3K36. (isaac2007interactionofepe1 pages 1-2, raiymbek2019anonenzymaticfunction pages 3-5, raiymbek2020anh3k9methylationdependent pages 5-6)
In fission yeast, H3K9 methylation (H3K9me) specifies silent chromatin/heterochromatin and supports recruitment of HP1 proteins, including Swi6, to establish and propagate repressed chromatin states at sites such as centromeres, telomeres, and the mating-type locus. Epe1 operates within this H3K9me/Swi6-marked chromatin landscape as a factor that restrains heterochromatin spreading and influences epigenetic stability. (raiymbek2020anh3k9methylationdependent pages 2-3, raiymbek2020anh3k9methylationdependent pages 5-6, raiymbek2020anh3k9methylationdependent pages 1-2)
Epe1 is best described as an anti-silencing/heterochromatin-restriction factor: loss of Epe1 can increase heterochromatin spreading beyond boundaries and alter the distribution of H3K9 methylation, while overexpression can disrupt heterochromatin. (isaac2007interactionofepe1 pages 1-2, raiymbek2020anh3k9methylationdependent pages 2-3)
Multiple studies report that Epe1 contains a JmjC-like domain and additional regulatory regions:
- Sorida et al. describe a distinct N-terminal transcriptional activation (NTA) domain (approximately residues 1–171, with activity extending to ~208) and a C-terminal Swi6-binding region (approximately residues 487–948). (sorida2019regulationofectopic pages 12-13, sorida2019regulationofectopic pages 1-2)
- Earlier work mapped the JmjC region to the C-terminus (cDNA spanning roughly aa 652 to the C-terminus) and found separability between Swi6 interaction and JmjC-dependent function. (trewick2007thejmjcdomain pages 1-3)
Epe1’s JmjC-like motif is non-canonical in sequence and/or cofactor coordination:
- Isaac et al. note Epe1’s JmjC domain lacks conservation of Fe(II)-binding residues and that no demethylase activity was detected, arguing against a canonical Fe(II)/2-oxoglutarate demethylase mechanism. (isaac2007interactionofepe1 pages 1-2)
- Raiymbek et al. (and related mechanistic work) highlight that Epe1 has a non-canonical HXE…Y motif and a histidine-to-tyrosine substitution (Y370) at a position typically associated with iron coordination in canonical JmjC demethylases. (raiymbek2020anh3k9methylationdependent pages 3-5, raiymbek2020anh3k9methylationdependent pages 2-3, raiymbek2019anonenzymaticfunction pages 1-3)
Current evidence does not establish a definitive biochemical substrate in vitro.
- Several studies report no detectable in vitro H3K9 demethylase activity, even though mutations in residues predicted to coordinate Fe(II) or 2-oxoglutarate affect Epe1 function in vivo. (trewick2007thejmjcdomain pages 11-12, raiymbek2020anh3k9methylationdependent pages 2-3, raiymbek2019anonenzymaticfunction pages 5-6)
- Trewick et al. interpret the requirement for predicted cofactor-binding residues as consistent with a 2-OG/Fe(II)-dependent dioxygenase, and suggest Epe1 could be a protein hydroxylase affecting stability or interactions of heterochromatin proteins rather than a classic histone demethylase. (trewick2007thejmjcdomain pages 11-12)
- Sorida et al. provide in vivo genetic evidence that the JmjC module contributes to removal of established ectopic heterochromatin, while a non-enzymatic NTA function prevents de novo ectopic H3K9me deposition. (sorida2019regulationofectopic pages 1-2, sorida2019regulationofectopic pages 12-13)
Interpretation: A conservative functional annotation supported by the corpus is that Epe1 is a JmjC-family, non-canonical dioxygenase-like protein whose dominant demonstrated role is non-enzymatic regulation of heterochromatin; whether it catalyzes histone demethylation, hydroxylation of non-histone substrates, or context-specific modification remains unresolved in vitro. (raiymbek2020anh3k9methylationdependent pages 2-3, isaac2007interactionofepe1 pages 1-2, trewick2007thejmjcdomain pages 11-12)
Epe1 is predominantly nuclear and enriched at constitutive heterochromatin foci, recruited through Swi6/HP1 and dependent on H3K9 methylation machinery:
- Epe1 co-localizes with Swi6 at pericentromeric dg/dh repeats, telomeres, and the mating-type locus; disrupting JmjC/cofactor-binding residues (e.g., H297A, Y307A, Y370A) impairs Swi6 binding and produces diffuse nuclear localization with reduced chromatin occupancy. (raiymbek2020anh3k9methylationdependent pages 5-6, raiymbek2020anh3k9methylationdependent pages 3-5)
- Under stress, proteasome-mediated truncation yields tEpe1, which shows increased cytoplasmic localization and reduced chromatin association, functionally shifting the heterochromatin landscape. (yaseen2022proteasomedependenttruncationof pages 9-11, yaseen2022proteasomedependenttruncationof pages 8-9, yaseen2022proteasomedependenttruncationof pages 6-8)
A central mechanistic model supported by biochemical and genetic evidence is that Epe1’s anti-silencing function is mediated through H3K9me-stimulated interaction with Swi6/HP1, leading to antagonism of histone deacetylation:
- Epe1’s C-terminus directly binds Swi6, and H3K9 methylation stimulates this interaction in vitro and in vivo. (raiymbek2020anh3k9methylationdependent pages 1-2, raiymbek2020anh3k9methylationdependent pages 20-22)
- Expressing Epe1’s C-terminus can disrupt heterochromatin by outcompeting/displacing the histone deacetylase Clr3 from heterochromatin. (raiymbek2020anh3k9methylationdependent pages 1-2, raiymbek2020anh3k9methylationdependent pages 20-22)
This frames Epe1 as a regulator of heterochromatin complex assembly rather than only an “eraser” enzyme. (raiymbek2020anh3k9methylationdependent pages 2-3, raiymbek2020anh3k9methylationdependent pages 20-22)
Sorida et al. propose a separation-of-function organization:
- The NTA domain is required to prevent stochastic de novo ectopic H3K9 methylation and variegation.
- The JmjC module is required for efficient removal of established ectopic heterochromatin in vivo.
This dual model reconciles earlier “putative demethylase” expectations with later non-enzymatic interaction models. (sorida2019regulationofectopic pages 1-2, sorida2019regulationofectopic pages 12-13)
Bao et al. (2022) provide a mechanistic link between nutrient status and Epe1 abundance:
- Disruption of cAMP signaling (e.g., git3Δ) nearly abolishes polysome-associated epe1+ mRNA, indicating reduced translation; git3Δ cgs1Δ partially restores polysome loading.
- Cycloheximide-chase indicates similar degradation rates over 45 minutes, supporting translation control rather than altered proteolysis.
- Reduced Epe1 under low glucose correlates with increased H3K9me2 at heterochromatin islands.
These data indicate that Epe1 is a regulated “tunable knob” coupling metabolism to heterochromatin state. (bao2022thecampsignaling pages 8-9, bao2022thecampsignaling pages 12-13, bao2022thecampsignaling pages 6-8)
Yaseen et al. (2022) connect Epe1 regulation to adaptive phenotypes under stress:
- Stressors (caffeine, azoles) induce ubiquitylation and proteasome-dependent removal of the N-terminal ~150 residues, producing tEpe1.
- Truncation is regulated by the cell integrity MAPK pathway (Pek1/Pmk1).
- Dynamics include tEpe1 appearing after ~7 h in 14 mM caffeine, and becoming undetectable ~9 h after caffeine removal (with recovery requiring new protein synthesis).
- Truncated Epe1 accumulates more in the cytoplasm, reduces normal heterochromatin foci, and correlates with increased H3K9 methylation at facultative islands and increased resistance frequencies (quantified as resistant colonies per 1×10^4 viable cells plated).
- Among caffeine-resistant Epe1ΔN150 isolates, 8/10 showed increased H3K9me2 at isl14/ncRNA394.
This work provides a concrete molecular mechanism linking environmental stress to Epe1 functional attenuation and epigenetic diversification relevant to antifungal resistance. (yaseen2022proteasomedependenttruncationof pages 2-4, yaseen2022proteasomedependenttruncationof pages 1-2, yaseen2022proteasomedependenttruncationof pages 8-9, yaseen2022proteasomedependenttruncationof pages 21-25)
Common experimental readouts include reporter-based silencing (ura4+/ade6+ reporters), colony color variegation, ChIP(-seq) for H3K9me and Swi6/HP1, RNA-seq/RT-qPCR for heterochromatin transcripts, and localization by microscopy.
Key phenotype patterns:
- Loss of Epe1 (epe1Δ): increased heterochromatin spreading/boundary defects and epigenetic variability; can also alleviate silencing within certain heterochromatin contexts depending on locus and boundary state. (isaac2007interactionofepe1 pages 1-2, raiymbek2020anh3k9methylationdependent pages 2-3)
- Epe1 overexpression: disrupts heterochromatin (anti-silencing becomes excessive), a phenotype used for genetic suppression screens that identified cAMP pathway regulators. (bao2022thecampsignaling pages 2-3, bao2022thecampsignaling pages 3-6)
Larkin et al. (Developmental Cell, Aug 2024) used an inducible epe1deg system to measure timescales and dynamics during heterochromatin misregulation:
- Epe1 protein becomes undetectable within ~30 minutes and epe1 mRNA drops ~8-fold after induction.
- In mst2Δ epe1deg backgrounds, clr4+ mRNA can decrease ~4-fold, and adaptive H3K9me develops de novo over clr4+.
- The system shows a stress phase of ~24–48 h followed by adaptation by ~120 h.
- Epigenetic “memory” persists for ~24 h (~6–8 generations) after stress removal; 48–72 h recovery erases memory.
- Quantitative colony area statistics across the timecourse are reported (e.g., 0 h: 34.5 ± 27.3; 120 h: 118.9 ± 37.6 pixels², etc.).
These results elevate Epe1 from a static boundary factor to a dynamically regulated controller of population-level epigenetic adaptation. (larkin2024mappingthedynamics pages 5-7, larkin2024mappingthedynamics pages 24-26, larkin2024mappingthedynamics pages 26-29)
Takahata et al. (Genes to Cells, Jun 2024) show that increasing FACT chromatin binding and suppressing histone turnover (via Pob3–Nhp6 fusions) stabilizes heterochromatin and suppresses epe1Δ-associated variegation:
- Using a dg::ade6+ reporter, epe1Δ displayed a silencing defect in ~40% of colonies (pink/white), while a strengthened FACT context suppressed this variegation.
- ChIP shows 2–3-fold increases in H3K9me and HP1/Swi6 at pericentromeric regions with the PN(x3) condition.
This provides a mechanistic lever—histone turnover control/FACT recruitment—that functionally compensates for Epe1-linked instability and supports the view that Epe1 participates in balancing heterochromatin stability versus plasticity. (takahata2024thehmg‐boxmodule pages 11-11)
A 2023 review emphasizes how heterochromatin relies on effector complexes such as FACT recruited by Swi6/HP1, while also noting Epe1’s association with Swi6 and role in stimulating heterochromatic ncRNA transcription relevant to RNAi-linked heterochromatin processes. (takahata2023opposingrolesof pages 8-10, takahata2023opposingrolesof pages 6-8)
Although Epe1 itself is studied in a model organism, the work has direct “real-world” relevance in two main ways:
1. Epigenetic adaptation/resistance models: Stress-induced truncation and relocalization of Epe1 creates a mechanistic model for how transient, heterochromatin-dependent epimutations can generate drug resistance in fungal lineages, informing strategies to counter antifungal resistance by targeting signaling (CIP MAPK) or proteasome-dependent processing pathways. (yaseen2022proteasomedependenttruncationof pages 1-2, yaseen2022proteasomedependenttruncationof pages 8-9)
2. Synthetic/engineering approaches to chromatin state control: Recent FACT-engineering work demonstrates that altering chromatin-binding modules can modulate heterochromatin formation rates and suppress variegation arising from Epe1 loss, illustrating experimentally tractable routes to stabilize/reshape epigenetic states in vivo. (takahata2024thehmg‐boxmodule pages 11-11, takahata2024thehmg‐boxmodule pages 1-2)
Across influential mechanistic studies, Epe1 is repeatedly characterized as “putative” for histone demethylase activity, with in vitro demethylation frequently undetectable but with strong genetic requirements for residues typically associated with JmjC cofactor binding. This supports two plausible interpretations:
- Epe1 has latent or context-dependent enzymatic activity that requires additional factors or specific chromatin context not recapitulated in simplified in vitro assays.
- The JmjC fold in Epe1 primarily supports structural/allosteric regulation and protein–protein interactions, and its “cofactor-binding residues” are repurposed for conformational control of non-enzymatic anti-silencing. (raiymbek2020anh3k9methylationdependent pages 2-3, trewick2007thejmjcdomain pages 11-12)
The combined 2022–2024 literature positions Epe1 as a regulated antagonist of heterochromatin spreading that can be tuned by nutrient signaling (cAMP–PKA translation) or stress (proteasome truncation), enabling cells to switch between stable silencing and adaptive epigenetic diversification. (bao2022thecampsignaling pages 8-9, yaseen2022proteasomedependenttruncationof pages 2-4, larkin2024mappingthedynamics pages 26-29)
The following table consolidates key findings, assays, quantitative data, URLs, and publication dates.
| Claim/finding | Mechanism/domain | Key assays/quantitative data | Source (authors, year, journal) | URL | Pub date |
|---|---|---|---|---|---|
| Identity verified: target is Schizosaccharomyces pombe Epe1/Jhd1, ORF SPCC622.16c, a JmjC-family chromatin regulator that localizes to heterochromatin via Swi6/HP1 rather than the budding-yeast Jhd1 KDM | JmjC-domain protein; heterochromatin-enriched through Swi6/HP1 interaction; anti-silencing factor at centromeres, telomeres, mating-type locus | Localization/co-IP genetics place Epe1 at constitutive heterochromatin; loss causes spreading beyond boundaries and altered silencing; overexpression disrupts heterochromatin (isaac2007interactionofepe1 pages 1-2, raiymbek2019anonenzymaticfunction pages 5-6, raiymbek2020anh3k9methylationdependent pages 5-6) | Isaac et al., 2007, Genetics; Raiymbek et al., 2020, eLife | https://doi.org/10.1534/genetics.106.068684 ; https://doi.org/10.7554/eLife.53155 | Apr 2007; Mar 2020 |
| Restricts heterochromatin spread and supports chromatin boundary function | Anti-silencing activity at heterochromatin edges; recruited by Swi6/HP1; function linked to JmjC integrity but not clearly to proven in vitro demethylation | epe1Δ enhances silencing at heterochromatin edges, promotes spreading across boundaries, partially suppresses clr defects, and causes broad transcriptional changes; classic phenotype is expansion of silent chromatin into neighboring euchromatin while also destabilizing normal heterochromatin domains (isaac2007interactionofepe1 pages 1-2, raiymbek2020anh3k9methylationdependent pages 2-3) | Isaac et al., 2007, Genetics; Raiymbek et al., 2020, eLife | https://doi.org/10.1534/genetics.106.068684 ; https://doi.org/10.7554/eLife.53155 | Apr 2007; Mar 2020 |
| Dual role: prevention of ectopic heterochromatin is partly non-enzymatic, while removal of established ectopic H3K9me depends on the JmjC module | N-terminal transcriptional activation (NTA) domain prevents de novo ectopic H3K9me; JmjC domain contributes to erasure/removal of established H3K9 methylation | Sorida et al. define NTA ~aa 1–171 (activity extending to ~208 aa) and a C-terminal Swi6-binding region aa 487–948; H297A JmjC mutant suppresses variegation/prevents de novo ectopic deposition but fails to efficiently remove established ectopic heterochromatin; single-copy Epe1 removes H3K9me at some loci, overexpression removes it more broadly (sorida2019regulationofectopic pages 1-2, sorida2019regulationofectopic pages 12-13) | Sorida et al., 2019, PLOS Genetics | https://doi.org/10.1371/journal.pgen.1008129 | Jun 2019 |
| Epe1 has strong non-enzymatic anti-silencing activity through methylation-dependent interaction with Swi6/HP1 and displacement of Clr3 HDAC | JmjC/cofactor-binding residues regulate conformation and Swi6/HP1 binding; C-terminus directly binds Swi6; Epe1-Swi6 complex antagonizes Clr3-mediated hypoacetylation | Purified Epe1 showed no detectable H3K9 demethylase activity in vitro; JmjC cofactor mutants (H297A, Y307A, Y370A) lose Swi6 binding/localization; Epe1 C-terminus is sufficient to displace Clr3 from heterochromatin and disrupt silencing (raiymbek2020anh3k9methylationdependent pages 2-3, raiymbek2020anh3k9methylationdependent pages 1-2, raiymbek2019anonenzymaticfunction pages 5-6, raiymbek2020anh3k9methylationdependent pages 20-22, raiymbek2020anh3k9methylationdependent pages 5-6) | Raiymbek et al., 2020, eLife | https://doi.org/10.7554/eLife.53155 | Mar 2020 |
| cAMP-PKA signaling regulates Epe1 abundance mainly at the translation step, linking nutrient signaling to heterochromatin state | Git3/Gpa/Cyr1 → cAMP → Pka1 promotes efficient translation of epe1+ mRNA; effect is post-transcriptional and largely independent of altered protein degradation | In git3Δ, polysome-associated epe1+ mRNA is nearly abolished; git3Δ cgs1Δ partially restores polysome loading; cycloheximide chase shows similar Epe1 degradation over 45 min, arguing against stability control; low glucose for 6 h lowers Epe1 protein and increases H3K9me2 at many heterochromatin islands; SacI::ade6+ silencing in git3Δ gives red/pink colonies but weaker than epe1Δ (bao2022thecampsignaling pages 6-8, bao2022thecampsignaling pages 12-13, bao2022thecampsignaling pages 8-9, bao2022thecampsignaling pages 9-12, bao2022thecampsignaling pages 1-2) | Bao et al., 2022, PLOS Genetics | https://doi.org/10.1371/journal.pgen.1010049 | Feb 2022 |
| Stress triggers proteasome-dependent Epe1 truncation to tEpe1, reducing nuclear/chromatin association and promoting adaptive H3K9 methylation | Regulated ubiquitin/proteasome processing removes ~N-terminal 150 aa; requires cell integrity pathway (CIP) MAPK components Pek1/Pmk1; truncated protein accumulates more in cytoplasm | tEpe1 appears after ~7 h at 14 mM caffeine and after 16 h at 5–15 mM caffeine; disappears ~9 h after caffeine removal; cleavage signal maps to aa 100–150, and deleting aa 101–110 blocks cleavage; proteomics found 23 proteasome subunits enriched with Epe1 after caffeine; 8/10 caffeine-resistant Epe1ΔN150 isolates showed higher H3K9me2 at isl14/ncRNA394; resistance quantified as resistant colonies per 1×10^4 viable cells plated (yaseen2022proteasomedependenttruncationof pages 9-11, yaseen2022proteasomedependenttruncationof pages 21-25, yaseen2022proteasomedependenttruncationof pages 8-9, yaseen2022proteasomedependenttruncationof pages 2-4, yaseen2022proteasomedependenttruncationof pages 1-2, yaseen2022proteasomedependenttruncationof pages 6-8) | Yaseen et al., 2022, Nature Structural & Molecular Biology | https://doi.org/10.1038/s41594-022-00801-y | Jul 2022 |
| 2024 work shows rapid Epe1 loss can drive multi-day epigenetic adaptation and short-term memory of heterochromatin misregulation | Acute Epe1 depletion unleashes H3K9me spreading; adaptive silencing targets clr4+ and nearby loci; memory depends on residual H3K9 methylation and is modulated by chromatin factors such as Red1 and Gcn5 | Inducible epe1deg gives complete loss of detectable protein within ~30 min and ~8-fold mRNA reduction; in mst2Δ epe1deg, clr4+ mRNA falls ~4-fold; stress phase spans 24–48 h, adaptation evident by ~120 h; short recovery of 24 h preserves partial memory, whereas 48–72 h recovery erases it; colony area stats: 0 h 34.5 ± 27.3, 120 h 118.9 ± 37.6, 144 h 87.3 ± 59.4, 168 h 26.3 ± 25.9 pixels²; adaptive memory persists ~24 h (~6–8 generations) after stress removal (larkin2024mappingthedynamics pages 32-35, larkin2024mappingthedynamics pages 5-7, larkin2024mappingthedynamics pages 24-26, larkin2024mappingthedynamics pages 26-29, larkin2024mappingthedynamics pages 22-24, larkin2024mappingthedynamics pages 13-15, larkin2024mappingthedynamics pages 18-19) | Larkin et al., 2024, Developmental Cell | https://doi.org/10.1016/j.devcel.2024.07.006 | Aug 2024 |
| 2024 FACT engineering study shows stronger FACT recruitment can suppress epe1Δ-associated heterochromatin variegation | Pob3-Nhp6 fusion [PN(x3)] enhances FACT chromatin binding, histone-turnover repression, H3K9 methylation, and Swi6 enrichment; FACT acts upstream of Epe1-linked variegation | On dg::ade6+, epe1Δ showed silencing defect in ~40% of colonies (pink/white); pn(x3) strongly suppressed this variegation; ChIP at pericentromeric imr/dh showed 2–3-fold increases in H3K9me and HP1/Swi6 with pn(x3); colony scoring used ~400 colonies/condition, with ChIP typically n=3 (takahata2024thehmg‐boxmodule pages 11-11, takahata2024thehmg‐boxmodule pages 9-9, takahata2024thehmg‐boxmodule pages 11-12) | Takahata et al., 2024, Genes to Cells | https://doi.org/10.1111/gtc.13132 | Jun 2024 |
Table: This table compiles key functional-annotation evidence for Schizosaccharomyces pombe Epe1/Jhd1 (UniProt O94603), including mechanism, localization, pathway context, and the most informative quantitative results. It is useful as a citation-ready summary spanning foundational studies through 2024 advances.
References
(sorida2019regulationofectopic pages 1-2): Masato Sorida, Takahiro Hirauchi, Hiroaki Ishizaki, Wataru Kaito, Atsushi Shimada, Chie Mori, Yuji Chikashige, Yasushi Hiraoka, Yutaka Suzuki, Yasuyuki Ohkawa, Hiroaki Kato, Shinya Takahata, and Yota Murakami. Regulation of ectopic heterochromatin-mediated epigenetic diversification by the jmjc family protein epe1. PLOS Genetics, 15:e1008129, Jun 2019. URL: https://doi.org/10.1371/journal.pgen.1008129, doi:10.1371/journal.pgen.1008129. This article has 33 citations and is from a domain leading peer-reviewed journal.
(isaac2007interactionofepe1 pages 1-2): Sara Isaac, Julian Walfridsson, Tal Zohar, David Lazar, Tamar Kahan, Karl Ekwall, and Amikam Cohen. Interaction of epe1 with the heterochromatin assembly pathway in schizosaccharomyces pombe. Genetics, 175:1549-1560, Apr 2007. URL: https://doi.org/10.1534/genetics.106.068684, doi:10.1534/genetics.106.068684. This article has 53 citations and is from a domain leading peer-reviewed journal.
(raiymbek2020anh3k9methylationdependent pages 2-3): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Ajay Larkin, Saikat Biswas, Raymond C Trievel, Uhn-soo Cho, and Kaushik Ragunathan. An h3k9 methylation-dependent protein interaction regulates the non-enzymatic functions of a putative histone demethylase. eLife, Mar 2020. URL: https://doi.org/10.7554/elife.53155, doi:10.7554/elife.53155. This article has 39 citations and is from a domain leading peer-reviewed journal.
(raiymbek2020anh3k9methylationdependent pages 20-22): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Ajay Larkin, Saikat Biswas, Raymond C Trievel, Uhn-soo Cho, and Kaushik Ragunathan. An h3k9 methylation-dependent protein interaction regulates the non-enzymatic functions of a putative histone demethylase. eLife, Mar 2020. URL: https://doi.org/10.7554/elife.53155, doi:10.7554/elife.53155. This article has 39 citations and is from a domain leading peer-reviewed journal.
(yaseen2022proteasomedependenttruncationof pages 8-9): Imtiyaz Yaseen, Sharon A. White, Sito Torres-Garcia, Christos Spanos, Marcel Lafos, Elisabeth Gaberdiel, Rebecca Yeboah, Meriem El Karoui, Juri Rappsilber, Alison L. Pidoux, and Robin C. Allshire. Proteasome-dependent truncation of the negative heterochromatin regulator epe1 mediates antifungal resistance. Jul 2022. URL: https://doi.org/10.1038/s41594-022-00801-y, doi:10.1038/s41594-022-00801-y. This article has 22 citations and is from a highest quality peer-reviewed journal.
(bao2022thecampsignaling pages 8-9): Kehan Bao, Chun-Min Shan, Xiao Chen, Gulzhan Raiymbek, Jeremy G. Monroe, Yimeng Fang, Takenori Toda, Kristin S. Koutmou, Kaushik Ragunathan, Chao Lu, Luke E. Berchowitz, and Songtao Jia. The camp signaling pathway regulates epe1 protein levels and heterochromatin assembly. PLOS Genetics, 18(2):e1010049, Feb 2022. URL: https://doi.org/10.1371/journal.pgen.1010049, doi:10.1371/journal.pgen.1010049. This article has 14 citations and is from a domain leading peer-reviewed journal.
(larkin2024mappingthedynamics pages 5-7): Ajay Larkin, Colin Kunze, Melissa Seman, Alexander Levashkevich, Justin Curran, Dionysus Morris-Evans, Sophia Lemieux, Ahmad S. Khalil, and Kaushik Ragunathan. Mapping the dynamics of epigenetic adaptation in s. pombe during heterochromatin misregulation. Developmental Cell, 59:2222-2238.e4, Aug 2024. URL: https://doi.org/10.1016/j.devcel.2024.07.006, doi:10.1016/j.devcel.2024.07.006. This article has 10 citations and is from a highest quality peer-reviewed journal.
(raiymbek2019anonenzymaticfunction pages 3-5): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Raymond Trievel, Uhn-soo Cho, and Kaushik Ragunathan. A non-enzymatic function associated with a putative histone demethylase licenses epigenetic inheritance. bioRxiv, Feb 2019. URL: https://doi.org/10.1101/545814, doi:10.1101/545814. This article has 0 citations.
(raiymbek2020anh3k9methylationdependent pages 5-6): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Ajay Larkin, Saikat Biswas, Raymond C Trievel, Uhn-soo Cho, and Kaushik Ragunathan. An h3k9 methylation-dependent protein interaction regulates the non-enzymatic functions of a putative histone demethylase. eLife, Mar 2020. URL: https://doi.org/10.7554/elife.53155, doi:10.7554/elife.53155. This article has 39 citations and is from a domain leading peer-reviewed journal.
(raiymbek2020anh3k9methylationdependent pages 1-2): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Ajay Larkin, Saikat Biswas, Raymond C Trievel, Uhn-soo Cho, and Kaushik Ragunathan. An h3k9 methylation-dependent protein interaction regulates the non-enzymatic functions of a putative histone demethylase. eLife, Mar 2020. URL: https://doi.org/10.7554/elife.53155, doi:10.7554/elife.53155. This article has 39 citations and is from a domain leading peer-reviewed journal.
(sorida2019regulationofectopic pages 12-13): Masato Sorida, Takahiro Hirauchi, Hiroaki Ishizaki, Wataru Kaito, Atsushi Shimada, Chie Mori, Yuji Chikashige, Yasushi Hiraoka, Yutaka Suzuki, Yasuyuki Ohkawa, Hiroaki Kato, Shinya Takahata, and Yota Murakami. Regulation of ectopic heterochromatin-mediated epigenetic diversification by the jmjc family protein epe1. PLOS Genetics, 15:e1008129, Jun 2019. URL: https://doi.org/10.1371/journal.pgen.1008129, doi:10.1371/journal.pgen.1008129. This article has 33 citations and is from a domain leading peer-reviewed journal.
(trewick2007thejmjcdomain pages 1-3): Sarah C Trewick, Elsa Minc, Richard Antonelli, Takeshi Urano, and Robin C Allshire. The jmjc domain protein epe1 prevents unregulated assembly and disassembly of heterochromatin. The EMBO Journal, 26:4670-4682, Oct 2007. URL: https://doi.org/10.1038/sj.emboj.7601892, doi:10.1038/sj.emboj.7601892. This article has 125 citations.
(raiymbek2020anh3k9methylationdependent pages 3-5): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Ajay Larkin, Saikat Biswas, Raymond C Trievel, Uhn-soo Cho, and Kaushik Ragunathan. An h3k9 methylation-dependent protein interaction regulates the non-enzymatic functions of a putative histone demethylase. eLife, Mar 2020. URL: https://doi.org/10.7554/elife.53155, doi:10.7554/elife.53155. This article has 39 citations and is from a domain leading peer-reviewed journal.
(raiymbek2019anonenzymaticfunction pages 1-3): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Raymond Trievel, Uhn-soo Cho, and Kaushik Ragunathan. A non-enzymatic function associated with a putative histone demethylase licenses epigenetic inheritance. bioRxiv, Feb 2019. URL: https://doi.org/10.1101/545814, doi:10.1101/545814. This article has 0 citations.
(trewick2007thejmjcdomain pages 11-12): Sarah C Trewick, Elsa Minc, Richard Antonelli, Takeshi Urano, and Robin C Allshire. The jmjc domain protein epe1 prevents unregulated assembly and disassembly of heterochromatin. The EMBO Journal, 26:4670-4682, Oct 2007. URL: https://doi.org/10.1038/sj.emboj.7601892, doi:10.1038/sj.emboj.7601892. This article has 125 citations.
(raiymbek2019anonenzymaticfunction pages 5-6): Gulzhan Raiymbek, Sojin An, Nidhi Khurana, Saarang Gopinath, Raymond Trievel, Uhn-soo Cho, and Kaushik Ragunathan. A non-enzymatic function associated with a putative histone demethylase licenses epigenetic inheritance. bioRxiv, Feb 2019. URL: https://doi.org/10.1101/545814, doi:10.1101/545814. This article has 0 citations.
(yaseen2022proteasomedependenttruncationof pages 9-11): Imtiyaz Yaseen, Sharon A. White, Sito Torres-Garcia, Christos Spanos, Marcel Lafos, Elisabeth Gaberdiel, Rebecca Yeboah, Meriem El Karoui, Juri Rappsilber, Alison L. Pidoux, and Robin C. Allshire. Proteasome-dependent truncation of the negative heterochromatin regulator epe1 mediates antifungal resistance. Jul 2022. URL: https://doi.org/10.1038/s41594-022-00801-y, doi:10.1038/s41594-022-00801-y. This article has 22 citations and is from a highest quality peer-reviewed journal.
(yaseen2022proteasomedependenttruncationof pages 6-8): Imtiyaz Yaseen, Sharon A. White, Sito Torres-Garcia, Christos Spanos, Marcel Lafos, Elisabeth Gaberdiel, Rebecca Yeboah, Meriem El Karoui, Juri Rappsilber, Alison L. Pidoux, and Robin C. Allshire. Proteasome-dependent truncation of the negative heterochromatin regulator epe1 mediates antifungal resistance. Jul 2022. URL: https://doi.org/10.1038/s41594-022-00801-y, doi:10.1038/s41594-022-00801-y. This article has 22 citations and is from a highest quality peer-reviewed journal.
(bao2022thecampsignaling pages 12-13): Kehan Bao, Chun-Min Shan, Xiao Chen, Gulzhan Raiymbek, Jeremy G. Monroe, Yimeng Fang, Takenori Toda, Kristin S. Koutmou, Kaushik Ragunathan, Chao Lu, Luke E. Berchowitz, and Songtao Jia. The camp signaling pathway regulates epe1 protein levels and heterochromatin assembly. PLOS Genetics, 18(2):e1010049, Feb 2022. URL: https://doi.org/10.1371/journal.pgen.1010049, doi:10.1371/journal.pgen.1010049. This article has 14 citations and is from a domain leading peer-reviewed journal.
(bao2022thecampsignaling pages 6-8): Kehan Bao, Chun-Min Shan, Xiao Chen, Gulzhan Raiymbek, Jeremy G. Monroe, Yimeng Fang, Takenori Toda, Kristin S. Koutmou, Kaushik Ragunathan, Chao Lu, Luke E. Berchowitz, and Songtao Jia. The camp signaling pathway regulates epe1 protein levels and heterochromatin assembly. PLOS Genetics, 18(2):e1010049, Feb 2022. URL: https://doi.org/10.1371/journal.pgen.1010049, doi:10.1371/journal.pgen.1010049. This article has 14 citations and is from a domain leading peer-reviewed journal.
(yaseen2022proteasomedependenttruncationof pages 2-4): Imtiyaz Yaseen, Sharon A. White, Sito Torres-Garcia, Christos Spanos, Marcel Lafos, Elisabeth Gaberdiel, Rebecca Yeboah, Meriem El Karoui, Juri Rappsilber, Alison L. Pidoux, and Robin C. Allshire. Proteasome-dependent truncation of the negative heterochromatin regulator epe1 mediates antifungal resistance. Jul 2022. URL: https://doi.org/10.1038/s41594-022-00801-y, doi:10.1038/s41594-022-00801-y. This article has 22 citations and is from a highest quality peer-reviewed journal.
(yaseen2022proteasomedependenttruncationof pages 1-2): Imtiyaz Yaseen, Sharon A. White, Sito Torres-Garcia, Christos Spanos, Marcel Lafos, Elisabeth Gaberdiel, Rebecca Yeboah, Meriem El Karoui, Juri Rappsilber, Alison L. Pidoux, and Robin C. Allshire. Proteasome-dependent truncation of the negative heterochromatin regulator epe1 mediates antifungal resistance. Jul 2022. URL: https://doi.org/10.1038/s41594-022-00801-y, doi:10.1038/s41594-022-00801-y. This article has 22 citations and is from a highest quality peer-reviewed journal.
(yaseen2022proteasomedependenttruncationof pages 21-25): Imtiyaz Yaseen, Sharon A. White, Sito Torres-Garcia, Christos Spanos, Marcel Lafos, Elisabeth Gaberdiel, Rebecca Yeboah, Meriem El Karoui, Juri Rappsilber, Alison L. Pidoux, and Robin C. Allshire. Proteasome-dependent truncation of the negative heterochromatin regulator epe1 mediates antifungal resistance. Jul 2022. URL: https://doi.org/10.1038/s41594-022-00801-y, doi:10.1038/s41594-022-00801-y. This article has 22 citations and is from a highest quality peer-reviewed journal.
(bao2022thecampsignaling pages 2-3): Kehan Bao, Chun-Min Shan, Xiao Chen, Gulzhan Raiymbek, Jeremy G. Monroe, Yimeng Fang, Takenori Toda, Kristin S. Koutmou, Kaushik Ragunathan, Chao Lu, Luke E. Berchowitz, and Songtao Jia. The camp signaling pathway regulates epe1 protein levels and heterochromatin assembly. PLOS Genetics, 18(2):e1010049, Feb 2022. URL: https://doi.org/10.1371/journal.pgen.1010049, doi:10.1371/journal.pgen.1010049. This article has 14 citations and is from a domain leading peer-reviewed journal.
(bao2022thecampsignaling pages 3-6): Kehan Bao, Chun-Min Shan, Xiao Chen, Gulzhan Raiymbek, Jeremy G. Monroe, Yimeng Fang, Takenori Toda, Kristin S. Koutmou, Kaushik Ragunathan, Chao Lu, Luke E. Berchowitz, and Songtao Jia. The camp signaling pathway regulates epe1 protein levels and heterochromatin assembly. PLOS Genetics, 18(2):e1010049, Feb 2022. URL: https://doi.org/10.1371/journal.pgen.1010049, doi:10.1371/journal.pgen.1010049. This article has 14 citations and is from a domain leading peer-reviewed journal.
(larkin2024mappingthedynamics pages 24-26): Ajay Larkin, Colin Kunze, Melissa Seman, Alexander Levashkevich, Justin Curran, Dionysus Morris-Evans, Sophia Lemieux, Ahmad S. Khalil, and Kaushik Ragunathan. Mapping the dynamics of epigenetic adaptation in s. pombe during heterochromatin misregulation. Developmental Cell, 59:2222-2238.e4, Aug 2024. URL: https://doi.org/10.1016/j.devcel.2024.07.006, doi:10.1016/j.devcel.2024.07.006. This article has 10 citations and is from a highest quality peer-reviewed journal.
(larkin2024mappingthedynamics pages 26-29): Ajay Larkin, Colin Kunze, Melissa Seman, Alexander Levashkevich, Justin Curran, Dionysus Morris-Evans, Sophia Lemieux, Ahmad S. Khalil, and Kaushik Ragunathan. Mapping the dynamics of epigenetic adaptation in s. pombe during heterochromatin misregulation. Developmental Cell, 59:2222-2238.e4, Aug 2024. URL: https://doi.org/10.1016/j.devcel.2024.07.006, doi:10.1016/j.devcel.2024.07.006. This article has 10 citations and is from a highest quality peer-reviewed journal.
(takahata2024thehmg‐boxmodule pages 11-11): Shinya Takahata, Asahi Taguchi, Ayaka Takenaka, Miyuki Mori, Yuji Chikashige, Chihiro Tsutsumi, Yasushi Hiraoka, and Yota Murakami. The hmg‐box module in fact is critical for suppressing epigenetic variegation of heterochromatin in fission yeast. Genes to Cells, 29:567-583, Jun 2024. URL: https://doi.org/10.1111/gtc.13132, doi:10.1111/gtc.13132. This article has 2 citations and is from a peer-reviewed journal.
(takahata2023opposingrolesof pages 8-10): Shinya Takahata and Yota Murakami. Opposing roles of fact for euchromatin and heterochromatin in yeast. Biomolecules, Feb 2023. URL: https://doi.org/10.3390/biom13020377, doi:10.3390/biom13020377. This article has 4 citations.
(takahata2023opposingrolesof pages 6-8): Shinya Takahata and Yota Murakami. Opposing roles of fact for euchromatin and heterochromatin in yeast. Biomolecules, Feb 2023. URL: https://doi.org/10.3390/biom13020377, doi:10.3390/biom13020377. This article has 4 citations.
(takahata2024thehmg‐boxmodule pages 1-2): Shinya Takahata, Asahi Taguchi, Ayaka Takenaka, Miyuki Mori, Yuji Chikashige, Chihiro Tsutsumi, Yasushi Hiraoka, and Yota Murakami. The hmg‐box module in fact is critical for suppressing epigenetic variegation of heterochromatin in fission yeast. Genes to Cells, 29:567-583, Jun 2024. URL: https://doi.org/10.1111/gtc.13132, doi:10.1111/gtc.13132. This article has 2 citations and is from a peer-reviewed journal.
(bao2022thecampsignaling pages 9-12): Kehan Bao, Chun-Min Shan, Xiao Chen, Gulzhan Raiymbek, Jeremy G. Monroe, Yimeng Fang, Takenori Toda, Kristin S. Koutmou, Kaushik Ragunathan, Chao Lu, Luke E. Berchowitz, and Songtao Jia. The camp signaling pathway regulates epe1 protein levels and heterochromatin assembly. PLOS Genetics, 18(2):e1010049, Feb 2022. URL: https://doi.org/10.1371/journal.pgen.1010049, doi:10.1371/journal.pgen.1010049. This article has 14 citations and is from a domain leading peer-reviewed journal.
(bao2022thecampsignaling pages 1-2): Kehan Bao, Chun-Min Shan, Xiao Chen, Gulzhan Raiymbek, Jeremy G. Monroe, Yimeng Fang, Takenori Toda, Kristin S. Koutmou, Kaushik Ragunathan, Chao Lu, Luke E. Berchowitz, and Songtao Jia. The camp signaling pathway regulates epe1 protein levels and heterochromatin assembly. PLOS Genetics, 18(2):e1010049, Feb 2022. URL: https://doi.org/10.1371/journal.pgen.1010049, doi:10.1371/journal.pgen.1010049. This article has 14 citations and is from a domain leading peer-reviewed journal.
(larkin2024mappingthedynamics pages 32-35): Ajay Larkin, Colin Kunze, Melissa Seman, Alexander Levashkevich, Justin Curran, Dionysus Morris-Evans, Sophia Lemieux, Ahmad S. Khalil, and Kaushik Ragunathan. Mapping the dynamics of epigenetic adaptation in s. pombe during heterochromatin misregulation. Developmental Cell, 59:2222-2238.e4, Aug 2024. URL: https://doi.org/10.1016/j.devcel.2024.07.006, doi:10.1016/j.devcel.2024.07.006. This article has 10 citations and is from a highest quality peer-reviewed journal.
(larkin2024mappingthedynamics pages 22-24): Ajay Larkin, Colin Kunze, Melissa Seman, Alexander Levashkevich, Justin Curran, Dionysus Morris-Evans, Sophia Lemieux, Ahmad S. Khalil, and Kaushik Ragunathan. Mapping the dynamics of epigenetic adaptation in s. pombe during heterochromatin misregulation. Developmental Cell, 59:2222-2238.e4, Aug 2024. URL: https://doi.org/10.1016/j.devcel.2024.07.006, doi:10.1016/j.devcel.2024.07.006. This article has 10 citations and is from a highest quality peer-reviewed journal.
(larkin2024mappingthedynamics pages 13-15): Ajay Larkin, Colin Kunze, Melissa Seman, Alexander Levashkevich, Justin Curran, Dionysus Morris-Evans, Sophia Lemieux, Ahmad S. Khalil, and Kaushik Ragunathan. Mapping the dynamics of epigenetic adaptation in s. pombe during heterochromatin misregulation. Developmental Cell, 59:2222-2238.e4, Aug 2024. URL: https://doi.org/10.1016/j.devcel.2024.07.006, doi:10.1016/j.devcel.2024.07.006. This article has 10 citations and is from a highest quality peer-reviewed journal.
(larkin2024mappingthedynamics pages 18-19): Ajay Larkin, Colin Kunze, Melissa Seman, Alexander Levashkevich, Justin Curran, Dionysus Morris-Evans, Sophia Lemieux, Ahmad S. Khalil, and Kaushik Ragunathan. Mapping the dynamics of epigenetic adaptation in s. pombe during heterochromatin misregulation. Developmental Cell, 59:2222-2238.e4, Aug 2024. URL: https://doi.org/10.1016/j.devcel.2024.07.006, doi:10.1016/j.devcel.2024.07.006. This article has 10 citations and is from a highest quality peer-reviewed journal.
(takahata2024thehmg‐boxmodule pages 9-9): Shinya Takahata, Asahi Taguchi, Ayaka Takenaka, Miyuki Mori, Yuji Chikashige, Chihiro Tsutsumi, Yasushi Hiraoka, and Yota Murakami. The hmg‐box module in fact is critical for suppressing epigenetic variegation of heterochromatin in fission yeast. Genes to Cells, 29:567-583, Jun 2024. URL: https://doi.org/10.1111/gtc.13132, doi:10.1111/gtc.13132. This article has 2 citations and is from a peer-reviewed journal.
(takahata2024thehmg‐boxmodule pages 11-12): Shinya Takahata, Asahi Taguchi, Ayaka Takenaka, Miyuki Mori, Yuji Chikashige, Chihiro Tsutsumi, Yasushi Hiraoka, and Yota Murakami. The hmg‐box module in fact is critical for suppressing epigenetic variegation of heterochromatin in fission yeast. Genes to Cells, 29:567-583, Jun 2024. URL: https://doi.org/10.1111/gtc.13132, doi:10.1111/gtc.13132. This article has 2 citations and is from a peer-reviewed journal.