The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
Saccharomyces cerevisiae CHD1 encodes Chd1, a conserved SNF2-family ATP-dependent chromatin remodeller that uses ATP hydrolysis to translocate nucleosomal DNA and thereby slide and space nucleosomes, particularly over actively transcribed gene bodies. Yeast Chd1 functions in transcription-coupled chromatin reassembly/organization, suppressing cryptic internal transcription and helping maintain proper histone-modification domains near 5′ gene ends; its action is coordinated with elongation factors and histone chaperones (notably Paf1C/Rtf1 and FACT). Mechanistic understanding has been sharpened by structural biology (cryo-EM) and by 2023–2024 biophysical and sequencing-based assays that resolve stepwise and context-dependent sliding behaviors. (lee2017theatpdependentchromatin pages 1-2, sundaramoorthy2018structureofthe pages 1-5, park2023bidirectionalnucleosomesliding pages 1-2, murawska2011chdchromatinremodelers pages 6-7)
The evidence base summarized here is explicitly focused on yeast Chd1 and matches the UniProt target: S. cerevisiae Chd1 is described as a chromodomain-helicase-DNA-binding remodeler with tandem chromodomains, a bilobal Snf2-like ATPase motor, and a C-terminal DNA-binding module (SANT/SLIDE), consistent with UniProt P32657 annotations and the SNF2/RAD54 helicase-family assignment. The cryo-EM structure is specifically reported for Chd1 from the yeast Saccharomyces cerevisiae bound to a nucleosome. (sundaramoorthy2018structureofthe pages 1-5)
ATP-dependent chromatin remodellers are molecular motors that hydrolyse ATP to alter nucleosome position/structure and thereby regulate DNA accessibility. In yeast, Chd1 is classed among remodelers that can slide nucleosomes and generate regular spacing in nucleosomal arrays. (park2023bidirectionalnucleosomesliding pages 1-2, prajapati2020interplayamongatpdependent pages 1-3)
Yeast Chd1 is a monomeric, helicase-type ATPase chromatin remodeller that engages nucleosomal DNA with its ATPase motor at superhelix location 2 (SHL2), ~20 bp from the dyad, and shifts DNA around the histone core through a stepwise translocation cycle, repositioning nucleosomes along DNA. (park2023bidirectionalnucleosomesliding pages 1-2)
A cryo-EM structure of S. cerevisiae Chd1 bound to a nucleosome indicates that Chd1 can detach/unwrap ~two turns of nucleosomal DNA and binds in a catalytically poised configuration. The SANT/SLIDE DNA-binding region contacts detached/linker DNA while the ATPase engages at SHL2; chromodomain movements are linked to ATPase closure and catalysis. (sundaramoorthy2018structureofthe pages 1-5)
Complementary structural/biochemical analysis supports the importance of linker DNA engagement: Chd1 remodels in a state where its DNA-binding domain is positioned on linker DNA, and efficient repositioning depends on this DNA-binding region. (sundaramoorthy2018structureofthe pages 16-19)
Chd1 acts on nucleosomes (DNA wrapped on histone octamers) and is sensitive to extranucleosomal DNA context.
Quantitative and mechanistic observations include:
- Reported repositioning range: Chd1 can reposition nucleosomes 23–39 bp into a 54 bp linker (contextualized relative to ISW1a/ISW2). (sundaramoorthy2018structureofthe pages 16-19)
- In vitro array spacing: CHD1 establishes ~160 bp spacing, shorter than ISW1/INO80 (~175 bp) and ISW2 (~200 bp). (prajapati2020interplayamongatpdependent pages 5-8, prajapati2020interplayamongatpdependent media 42544443)
A 2023 high-resolution sliding study using both Widom 601 and a natural S. cerevisiae +1 nucleosome sequence (SWH1) shows that although Chd1 action at one SHL2 site is unidirectional, nucleosome symmetry allows back-and-forth (bi-directional) sliding when the enzyme acts on either side. The work also shows that DNA perturbations (poly(dA:dT), mismatches, single-nucleotide insertions) become preferentially positioned about one helical turn outside SHL2, and modeling indicates strong phasing can favor ~10 bp shifts. (park2023bidirectionalnucleosomesliding pages 1-2)
Yeast Chd1 is associated with transcribed gene bodies rather than promoters and is enriched over coding regions of active genes. (murawska2011chdchromatinremodelers pages 6-7)
Chd1 recruitment is linked to transcription elongation machinery:
- Genome-wide analyses indicate the PAF1 complex (Paf1C) is a key determinant of Chd1 recruitment to active genes, and Chd1 occupancy concords with RNAPII Ser5-phosphorylated patterns (an early elongation-associated form). (lee2017theatpdependentchromatin pages 1-2, lee2017theatpdependentchromatin pages 2-3)
- Spt4 (DSIF component) modulates recruitment; spt4Δ increases Chd1 binding near transcription start sites, consistent with negative modulation of 5′ recruitment. (lee2017theatpdependentchromatin pages 2-3)
- Rtf1 (Paf1C subunit) is implicated in Chd1 recruitment by earlier gene-level evidence and review synthesis. (murawska2011chdchromatinremodelers pages 6-7)
Direct interaction evidence (preprint; interpret cautiously): a 2024/2025 bioRxiv preprint maps a direct Rtf1–Chd1 interaction: a short N-terminal region of Rtf1 (aa 1–30) interacts with the Chd1 CHCT domain, supported by yeast two-hybrid mapping and alanine-scan disruption of key residues. The authors propose this interaction helps distribute Chd1 across transcribed genes and influences nucleosome positioning and cryptic transcription. (tripplehorn2025adirectinteraction pages 23-26, tripplehorn2025adirectinteraction pages 1-5)
Upstream coupling to DSIF is supported by a peer-reviewed mechanistic study showing that in S. cerevisiae a domain of Rtf1 directly interacts with the Spt5 CTR and is required for proper Paf1C recruitment to active genes, consistent with an indirect path by which DSIF→Paf1C could shape Chd1 positioning. (mayekar2013therecruitmentof pages 1-2)
Yeast chromatin organization reflects interplay among remodelers:
- ISW1 and CHD1 are described as major nucleosome-spacing enzymes that can compete to set nucleosome spacing; loss of both produces major disruption partly due to close-packed dinucleosomes. (prajapati2020interplayamongatpdependent pages 1-3)
- Genetic/functional synthesis indicates cryptic transcription and altered nucleosome spacing are exacerbated in chd1 isw1 double mutants, consistent with partially redundant roles in maintaining gene-body chromatin integrity. (murawska2011chdchromatinremodelers pages 6-7)
A genome-wide study reports that loss of CHD1 yields significantly aberrant H3K4me3/H3K36me3 patterns across ~half of the yeast genome, predominantly within ~1 kb of transcription start sites, with reciprocal changes between promoter-proximal (+1–+3) and more distal (+4–+6) nucleosomes. (lee2017theatpdependentchromatin pages 6-9)
Mechanistically, structural work suggests that Chd1-induced partial DNA unwrapping could alter display/accessibility of histone tail epitopes and thereby influence writer/eraser/reader enzymes, consistent with observed mark-boundary effects. (sundaramoorthy2018structureofthe pages 16-19)
CHD1 deletion is associated with altered co-transcriptional RNA processing:
- In one RNA-seq analysis, 35 introns were significantly affected, with 28/35 (80%) showing lower intron retention (improved splicing) in chd1Δ. (lee2017theatpdependentchromatin pages 6-9)
- Reanalysis with deeper RNA-seq indicated 94% of introns show lower intron retention in chd1Δ, with stronger effects in ribosomal protein genes where Chd1 is highly enriched. (lee2017theatpdependentchromatin pages 6-9)
These data support a model in which Chd1 influences elongation-coupled chromatin state and thereby indirectly impacts splicing efficiency. (lee2017theatpdependentchromatin pages 6-9)
Structural/biochemical work indicates that H2B K120 (yeast K123) ubiquitination can stimulate Chd1 activity ~2-fold in vitro and is enriched in coding regions. The same work discusses an estimated ~10% occupancy of the transiently unwrapped nucleosomal DNA state (baseline), and proposes that ubiquitin repositioning upon Chd1 binding stabilizes this unwrapped configuration, potentially enhancing DNA accessibility. (sundaramoorthy2018structureofthe pages 16-19)
Mimicking H3K36 trimethylation (via alkylation) modestly stimulates Chd1 activity, but the structural state captured did not show a stable direct interaction of the H3K36 region with the chromodomains, suggesting either weak/transient recognition or a requirement for alternative conformations. (sundaramoorthy2018structureofthe pages 16-19)
The 2023 Slide-seq study provides a modern mechanistic picture of how Chd1 integrates intrinsic DNA features and ATP-driven remodeling, including a concrete explanation for how a nominally unidirectional motor can yield bi-directional outcomes through nucleosome symmetry and repeated engagement of SHL2 sites. (park2023bidirectionalnucleosomesliding pages 1-2)
Two 2024 reviews summarize the field-wide shift toward a consensus “inside-the-box” translocation mechanism:
- A 2024 Biochemical Society Transactions review emphasizes that cryo-EM and single-molecule methods have only recently brought nucleosome-sliding mechanisms into focus and argues that CHD-family enzymes share a central remodeling mechanism with other remodelers, while auxiliary domains create family-specific behaviors. (reid2024howdoeschd4 pages 1-2)
- The same review synthesizes a stepwise model in which nucleotide-state changes in the RecA-like ATPase lobes produce incremental tracking-strand shifts and burst-like DNA release, and notes that comparable asymmetric stepping behaviors have been observed for multiple remodelers including CHD1 in related work (general, not yeast-specific). (reid2024howdoeschd4 pages 5-6)
- A 2024 biophysics-focused review highlights how cryo-EM and single-molecule FRET studies help explain apparent directional bias in remodeler action (including Chd1) as an emergent property of motor architecture plus substrate asymmetry (e.g., differential unwrapping propensity of the Widom 601 sequence). (klempahn2024chromatinremodelersa pages 2-5)
A high-level 2024 Nature Reviews Genetics synthesis (mammalian-focused) further underscores that structural/biochemical studies are increasingly defining how remodelers contact nucleosomes and other regulators; although not yeast-specific, it supports the broader interpretive framework for how remodeler specificity emerges from interaction surfaces and dynamic localization. (gourisankar2024contextspecificfunctionsof pages 1-3)
The most established “real-world implementation” of yeast CHD1 research is its use as a model system for chromatin remodeling mechanisms and for interpreting high-throughput chromatin maps. A yeast-focused review emphasizes yeast’s advantages (small genome, tractable mutants) for chromatin organization studies, including nucleosome spacing/phasing and remodeler competition models. (prajapati2020interplayamongatpdependent pages 5-8)
Chd1-dependent spacing/organization is directly relevant to:
- designing and interpreting MNase-seq/chemical mapping and nucleosome-repeat-length analyses (e.g., distinguishing remodeler-set spacing regimes), and
- conceptual engineering of transcriptional programs where chromatin reassembly and cryptic transcription suppression matter.
However, the retrieved literature does not establish a specific industrial/clinical deployment of yeast CHD1 itself; its application is primarily as a foundational mechanistic tool and model. (prajapati2020interplayamongatpdependent pages 5-8, murawska2011chdchromatinremodelers pages 6-7)
The following table compiles key functional claims with quantitative values and source types.
| Functional aspect | Key findings | Evidence type | Primary source(s) with year, DOI URL |
|---|---|---|---|
| Target identity / domain architecture | The literature matches Saccharomyces cerevisiae Chd1, the ATP-dependent chromatin remodeler encoded by CHD1/YER164W. Core architecture reported for yeast Chd1: tandem chromodomains, bilobal Snf2-family ATPase motor, and C-terminal SANT/SLIDE DNA-binding region; reviews also describe CHD-family flanking regulatory domains. This aligns with UniProt P32657 annotation as a SNF2/RAD54-family chromodomain helicase DNA-binding protein. (sundaramoorthy2018structureofthe pages 1-5, murawska2011chdchromatinremodelers pages 6-7) | Structural, review | Farnung et al., 2017, Nature, https://doi.org/10.1038/nature24046; Murawska & Brehm, 2011, Transcription, https://doi.org/10.4161/trns.2.6.17840 |
| Primary biochemical activity | Chd1 is an ATP-dependent chromatin remodeler that repositions/slides nucleosomes and spaces nucleosomal arrays. Chd1 acts on nucleosomal DNA at SHL2 (~20 bp from the dyad) and can assemble/reposition nucleosomes into evenly spaced arrays. (park2023bidirectionalnucleosomesliding pages 1-2) | Biochemical, mechanistic | Park et al., 2023, Nucleic Acids Research, https://doi.org/10.1093/nar/gkad738 |
| In vitro spacing specificity | In comparative in vitro spacing assays, CHD1 establishes the shortest average nucleosome spacing (~160 bp), compared with ~175 bp for ISW1/INO80 and ~200 bp for ISW2. Yeast average in vivo spacing is ~165 bp. (prajapati2020interplayamongatpdependent pages 5-8, prajapati2020interplayamongatpdependent media 42544443) | Review of primary spacing assays | Prajapati et al., 2020, Biology, https://doi.org/10.3390/biology9080190 |
| Structural mechanism on nucleosomes | Cryo-EM of S. cerevisiae Chd1 bound to the nucleosome shows the ATPase at SHL +2, the SANT/SLIDE DNA-binding region contacting linker DNA near SHL −7, and Chd1 detaching/unwrapping two turns of DNA from the histone octamer. This provides a direct structural explanation for ATP-coupled remodeling. (sundaramoorthy2018structureofthe pages 1-5) | Structural | Farnung et al., 2017, Nature, https://doi.org/10.1038/nature24046; Sundaramoorthy et al., 2018, eLife, https://doi.org/10.1101/290874 |
| Repositioning range / linker dependence | Text summarizing yeast Chd1 remodeling reports that Chd1 can reposition nucleosomes 23–39 bp into a 54 bp linker, similar to ISW1a/ISW2, supporting active engagement of extranucleosomal linker DNA by the DNA-binding domain. (sundaramoorthy2018structureofthe pages 16-19) | Structural discussion with prior biochemical reference | Sundaramoorthy et al., 2018, eLife, https://doi.org/10.1101/290874 |
| Sliding directionality | Chd1 translocates DNA unidirectionally toward the dyad from a single SHL2 site, but because nucleosomes have two symmetric SHL2 sites, the net outcome can be back-and-forth/bidirectional sliding. DNA perturbations tend to localize about one helical turn (~10 bp) outside SHL2, and strong phasing can favor ~10 bp shifts. (park2023bidirectionalnucleosomesliding pages 1-2) | Biophysical, sequencing-based mechanistic study | Park et al., 2023, Nucleic Acids Research, https://doi.org/10.1093/nar/gkad738 |
| DNA-sequence sensitivity / substrate preference | On the Widom 601 sequence, Chd1 preferentially shifts the dyad toward the TA-poor side; introducing long poly(dA:dT) tracts on that side reverses the preferred sliding direction. Similar principles were observed using the natural S. cerevisiae SWH1 +1 nucleosome sequence. (park2023bidirectionalnucleosomesliding pages 1-2) | Biophysical, substrate preference | Park et al., 2023, Nucleic Acids Research, https://doi.org/10.1093/nar/gkad738 |
| Cellular localization / chromatin context | Yeast Chd1 is enriched in the nucleus on transcribed gene bodies/coding regions, rather than promoters, and is associated with active transcription. It tracks especially well with highly transcribed genes and with RNAPII Ser5-phosphorylated occupancy patterns. (murawska2011chdchromatinremodelers pages 6-7, lee2017theatpdependentchromatin pages 1-2) | Genome-wide, review | Lee et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx636; Murawska & Brehm, 2011, Transcription, https://doi.org/10.4161/trns.2.6.17840 |
| Recruitment by elongation machinery | Recruitment is strongly linked to transcription elongation factors. Chd1 association decreases in Rtf1/PAF1C mutants, supporting recruitment by PAF1C; Spt4 can oppose/promote redistribution near 5′ ends depending on context. Chd1 also interacts functionally with FACT (Spt16-Pob3) and transcription elongation machinery. (murawska2011chdchromatinremodelers pages 6-7, lee2017theatpdependentchromatin pages 1-2, lee2017theatpdependentchromatin pages 2-3) | Genome-wide, genetic, review | Lee et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx636; Murawska & Brehm, 2011, Transcription, https://doi.org/10.4161/trns.2.6.17840 |
| Histone mark recognition / chromodomain function | In budding yeast, Chd1 contributes to maintaining H3K4me3/H3K36me3 domain boundaries, but Lee et al. report yeast Chd1 does not directly bind H3K4me3 the way human CHD1 can. A H3K36me3 mimic modestly stimulates Chd1 activity, but the structural study did not support a stable direct H3K36-tail interaction in the captured state. (lee2017theatpdependentchromatin pages 1-2, sundaramoorthy2018structureofthe pages 16-19) | Genome-wide, structural/biochemical | Lee et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx636; Sundaramoorthy et al., 2018, eLife, https://doi.org/10.1101/290874 |
| Modulation by H2B ubiquitination | H2BK120/K123 ubiquitination stimulates Chd1 activity ~2-fold in vitro. In the Chd1-bound unwrapped nucleosome, ubiquitin is repositioned toward DNA; the unwrapped nucleosome state is estimated to have ~10% occupancy in the absence of stabilizing factors, and ubiquitin is proposed to stabilize this transiently unwrapped state. Chd1 mutants also show reduced H2B ubiquitination. (sundaramoorthy2018structureofthe pages 1-5, sundaramoorthy2018structureofthe pages 16-19) | Structural, biochemical | Sundaramoorthy et al., 2018, eLife, https://doi.org/10.1101/290874 |
| Role in transcription-coupled chromatin restoration | Chd1 is thought to help re-establish nucleosome organization after RNA polymerase II passage, maintaining chromatin structure over coding regions and preventing inappropriate exposure of internal promoter-like DNA. (lee2017theatpdependentchromatin pages 1-2, park2023bidirectionalnucleosomesliding pages 1-2, murawska2011chdchromatinremodelers pages 6-7) | Genome-wide, mechanistic review | Lee et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx636; Murawska & Brehm, 2011, Transcription, https://doi.org/10.4161/trns.2.6.17840 |
| Cryptic transcription suppression | chd1 mutants show initiation from cryptic internal promoters; this defect is strongly enhanced in chd1 isw1 double mutants, indicating partially redundant roles of Chd1 and Isw1 in preserving coding-region chromatin integrity. (murawska2011chdchromatinremodelers pages 6-7, prajapati2020interplayamongatpdependent pages 1-3) | Genetic, review | Murawska & Brehm, 2011, Transcription, https://doi.org/10.4161/trns.2.6.17840; Prajapati et al., 2020, Biology, https://doi.org/10.3390/biology9080190 |
| Nucleosome organization phenotypes in mutants | Loss of both ISW1 and CHD1 causes major chromatin disruption and formation of close-packed dinucleosomes. chd1Δ alone reduces phasing beyond the +1 nucleosome, whereas double loss causes much stronger disorganization, especially on highly transcribed genes. (tripplehorn2025adirectinteraction pages 1-5, prajapati2020interplayamongatpdependent pages 1-3) | Genetic, review | Prajapati et al., 2020, Biology, https://doi.org/10.3390/biology9080190 |
| Effects on histone modification domains | Loss of CHD1 causes widespread, reciprocal disruption of H3K4me3 and H3K36me3 near the 5′ ends of genes, concentrated within ~1 kb of the TSS and affecting approximately half of the yeast genome. (lee2017theatpdependentchromatin pages 2-3, lee2017theatpdependentchromatin pages 6-9) | Genome-wide ChIP-seq / RNA-seq | Lee et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx636 |
| Effects on intron retention / splicing-linked transcription | RNA-seq showed 35 introns significantly affected in chd1Δ, with 28/35 (80%) showing lower intron retention (improved splicing). Reanalysis with deeper RNA-seq found 94% of introns had lower retention in chd1Δ, with the effect especially clear in ribosomal protein genes where Chd1 is enriched. (lee2017theatpdependentchromatin pages 6-9) | Genome-wide RNA-seq | Lee et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx636 |
| Relationship with FACT / other partners | Chd1 functionally interacts with FACT (Spt16-Pob3), PAF1 complex/Rtf1, and Spt4-Spt5 elongation factors; these interactions place Chd1 in the transcription-coupled chromatin reassembly pathway rather than acting primarily by changing RNAPII processivity directly. (lee2017theatpdependentchromatin pages 1-2, sundaramoorthy2018structureofthe pages 1-5, murawska2011chdchromatinremodelers pages 6-7) | Genome-wide, structural context, review | Lee et al., 2017, Nucleic Acids Research, https://doi.org/10.1093/nar/gkx636; Sundaramoorthy et al., 2018, eLife, https://doi.org/10.1101/290874; Murawska & Brehm, 2011, Transcription, https://doi.org/10.4161/trns.2.6.17840 |
Table: This table summarizes functional annotation evidence for Saccharomyces cerevisiae CHD1 (UniProt P32657), including biochemical activity, structural mechanism, recruitment, localization, mutant phenotypes, and key quantitative findings. It is useful as a compact evidence map linking specific claims to source types and DOI-resolved references.
Prajapati et al. (2020) Figure 4 summarizes how different yeast remodelers generate distinct nucleosome spacing in vitro, including the short spacing attributed to CHD1.
(prajapati2020interplayamongatpdependent media 42544443)
References
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(sundaramoorthy2018structureofthe pages 1-5): Ramasubramanian Sundaramoorthy, Amanda L. Hughes, Hassane El-Mkami, David Norman, and Tom Owen-Hughes. Structure of the chromatin remodelling enzyme chd1 bound to a ubiquitinylated nucleosome. eLife, Mar 2018. URL: https://doi.org/10.1101/290874, doi:10.1101/290874. This article has 100 citations and is from a domain leading peer-reviewed journal.
(park2023bidirectionalnucleosomesliding pages 1-2): Sangwoo Park, Giovanni B Brandani, Taekjip Ha, and Gregory D Bowman. Bi-directional nucleosome sliding by the chd1 chromatin remodeler integrates intrinsic sequence-dependent and atp-dependent nucleosome positioning. Nucleic Acids Research, 51:10326-10343, Sep 2023. URL: https://doi.org/10.1093/nar/gkad738, doi:10.1093/nar/gkad738. This article has 23 citations and is from a highest quality peer-reviewed journal.
(murawska2011chdchromatinremodelers pages 6-7): Magdalena Murawska and Alexander Brehm. Chd chromatin remodelers and the transcription cycle. Transcription, 2:244-253, Nov 2011. URL: https://doi.org/10.4161/trns.2.6.17840, doi:10.4161/trns.2.6.17840. This article has 162 citations and is from a peer-reviewed journal.
(prajapati2020interplayamongatpdependent pages 1-3): Hemant K. Prajapati, Josefina Ocampo, and David J. Clark. Interplay among atp-dependent chromatin remodelers determines chromatin organisation in yeast. Biology, 9:190, Jul 2020. URL: https://doi.org/10.3390/biology9080190, doi:10.3390/biology9080190. This article has 43 citations.
(prajapati2020interplayamongatpdependent pages 5-8): Hemant K. Prajapati, Josefina Ocampo, and David J. Clark. Interplay among atp-dependent chromatin remodelers determines chromatin organisation in yeast. Biology, 9:190, Jul 2020. URL: https://doi.org/10.3390/biology9080190, doi:10.3390/biology9080190. This article has 43 citations.
(sundaramoorthy2018structureofthe pages 16-19): Ramasubramanian Sundaramoorthy, Amanda L. Hughes, Hassane El-Mkami, David Norman, and Tom Owen-Hughes. Structure of the chromatin remodelling enzyme chd1 bound to a ubiquitinylated nucleosome. eLife, Mar 2018. URL: https://doi.org/10.1101/290874, doi:10.1101/290874. This article has 100 citations and is from a domain leading peer-reviewed journal.
(prajapati2020interplayamongatpdependent media 42544443): Hemant K. Prajapati, Josefina Ocampo, and David J. Clark. Interplay among atp-dependent chromatin remodelers determines chromatin organisation in yeast. Biology, 9:190, Jul 2020. URL: https://doi.org/10.3390/biology9080190, doi:10.3390/biology9080190. This article has 43 citations.
(lee2017theatpdependentchromatin pages 2-3): Yaelim Lee, Daechan Park, and Vishwanath R. Iyer. The atp-dependent chromatin remodeler chd1 is recruited by transcription elongation factors and maintains h3k4me3/h3k36me3 domains at actively transcribed and spliced genes. Nucleic Acids Research, 45:8646-8646, Jul 2017. URL: https://doi.org/10.1093/nar/gkx636, doi:10.1093/nar/gkx636. This article has 70 citations and is from a highest quality peer-reviewed journal.
(tripplehorn2025adirectinteraction pages 23-26): Sarah A. Tripplehorn, Margaret K. Shirra, Santana M. Lardo, Hannah G. Marvil, Sarah J. Hainer, and Karen M. Arndt. A direct interaction between the chd1 chct domain and rtf1 controls chd1 distribution and nucleosome positioning on active genes. bioRxiv, Dec 2025. URL: https://doi.org/10.1101/2024.12.06.627179, doi:10.1101/2024.12.06.627179. This article has 7 citations.
(tripplehorn2025adirectinteraction pages 1-5): Sarah A. Tripplehorn, Margaret K. Shirra, Santana M. Lardo, Hannah G. Marvil, Sarah J. Hainer, and Karen M. Arndt. A direct interaction between the chd1 chct domain and rtf1 controls chd1 distribution and nucleosome positioning on active genes. bioRxiv, Dec 2025. URL: https://doi.org/10.1101/2024.12.06.627179, doi:10.1101/2024.12.06.627179. This article has 7 citations.
(mayekar2013therecruitmentof pages 1-2): Manasi K. Mayekar, Richard G. Gardner, and Karen M. Arndt. The recruitment of the saccharomyces cerevisiae paf1 complex to active genes requires a domain of rtf1 that directly interacts with the spt4-spt5 complex. Molecular and Cellular Biology, 33:3259-3273, Aug 2013. URL: https://doi.org/10.1128/mcb.00270-13, doi:10.1128/mcb.00270-13. This article has 87 citations and is from a domain leading peer-reviewed journal.
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(gourisankar2024contextspecificfunctionsof pages 1-3): Sai Gourisankar, Andrey Krokhotin, Wendy Wenderski, and Gerald R. Crabtree. Context-specific functions of chromatin remodellers in development and disease. Nature Reviews Genetics, 25:340-361, Nov 2024. URL: https://doi.org/10.1038/s41576-023-00666-x, doi:10.1038/s41576-023-00666-x. This article has 75 citations and is from a domain leading peer-reviewed journal.