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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.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.
RLF2 is unambiguously the same budding-yeast gene as CAC1 (ordered locus YPR018W) and encodes the large, approximately 90-kDa subunit of chromatin assembly factor 1 (CAF-1). It is the yeast counterpart of metazoan CHAF1A/p150. The literature examined concerns Saccharomyces cerevisiae and is consistent with the supplied S288c/Q12495 record; no similarly named gene from another organism was substituted. Independent primary studies explicitly identify RLF2 with CAC1 and connect it to the large CAF-1 subunit. (kaufman1997ultravioletradiationsensitivity pages 1-2, enomoto1998chromatinassemblyfactor pages 1-2, enomoto1997rlf2asubunit pages 1-2)
Cac1/Rlf2 is not an enzyme and has no catalytic reaction or small-molecule substrate specificity. It is a nuclear histone-chaperone scaffold. In the heterotrimeric CAF-1 complex, it coordinates Cac2, Cac3/Msi1, histones H3–H4, DNA, and the sliding clamp PCNA. Its primary molecular function is to couple DNA synthesis to deposition of newly synthesized H3–H4, generating the tetrasome precursor of a nucleosome. This restores chromatin behind replication forks and at synthesis-dependent DNA-repair sites. (zhang2016adnabinding pages 1-2, mattiroli2017dnamediatedassociationof pages 1-2, mattiroli2017dnamediatedassociationof pages 4-6)
| Annotation aspect | Best-supported conclusion | Evidence type / strength | Key quantitative or mechanistic detail | Principal source / year |
|---|---|---|---|---|
| Identity | RLF2 is identical to CAC1 in Saccharomyces cerevisiae and encodes the large CAF-1 subunit; this matches the supplied Q12495/YPR018W identity. | Direct genetic and biochemical evidence; strong | Independently identified as the yeast counterpart of the human p150 CAF-1 subunit. | Kaufman et al., 1997; Enomoto et al., 1997; Enomoto & Berman, 1998 (kaufman1997ultravioletradiationsensitivity pages 1-2, enomoto1998chromatinassemblyfactor pages 1-2, enomoto1997rlf2asubunit pages 1-2) |
| Molecular class | Cac1/Rlf2 is a nonenzymatic histone chaperone and scaffold, not an enzyme; no catalytic reaction or conventional substrate specificity is known. | Biochemical reconstitution and structural studies; strong | It coordinates histone, DNA, PCNA, and CAF-1-subunit interactions to promote chromatin assembly. | Zhang et al., 2016; Mattiroli et al., 2017 (zhang2016adnabinding pages 1-2, mattiroli2017dnamediatedassociationof pages 1-2) |
| CAF-1 composition | Yeast CAF-1 is a heterotrimer of Cac1, Cac2, and Cac3/Msi1; Cac1 is the large structural and functional subunit. | Purification, sequence comparison, and reconstitution; strong | Cac1, Cac2, and Cac3 correspond broadly to human p150, p60, and p48-family subunits, respectively. | Kaufman et al., 1997; Mattiroli et al., 2017 (kaufman1997ultravioletradiationsensitivity pages 1-2, kaufman1997ultravioletradiationsensitivity pages 5-6, mattiroli2017dnamediatedassociationof pages 1-2) |
| Cargo and biological substrate | CAF-1 carries newly synthesized H3–H4 dimers and deposits an (H3–H4)₂ tetramer onto newly synthesized or repaired DNA. | Stoichiometric biochemistry; strong | One CAF-1 binds one H3–H4 dimer; a cross-linked tetramer binds two CAF-1 complexes, yielding an approximately 300-kDa species. | Mattiroli et al., 2017 (mattiroli2017dnamediatedassociationof pages 4-6) |
| Deposition mechanism | Histone binding activates Cac1 DNA engagement; two CAF-1·H3–H4 complexes meet on DNA, form the H3–H4 tetramer, and discharge it as a tetrasome. | EMSA, SEC-MALS, cross-linking, FRET, HX-MS, and assembly assays; strong | An 18-bp DNA bridges two WHDs; 33-bp DNA makes assembly tetramerization-dependent; 79-bp DNA supports complete histone discharge. Activity peaked at a twofold CAF-1 excess per H3–H4 tetramer. | Mattiroli et al., 2017 (mattiroli2017dnamediatedassociationof pages 10-12, mattiroli2017dnamediatedassociationof pages 2-4) |
| Domains and motifs | The supplied acidic CAF1A region and C-terminal Cac1-like domains agree with experimentally defined histone- and subunit-interaction regions and a C-terminal winged-helix DNA-binding domain. | Crystallography, mutagenesis, and biochemical binding; strong | Cac1 residues 520–606 form a WHD solved at 2.75 Å; DNA binding is sequence-independent. K564E/K568E disrupts the histone-activated DNA-bound intermediate without abolishing H3–H4 binding. | Zhang et al., 2016; Mattiroli et al., 2017 (zhang2016adnabinding pages 2-3, mattiroli2017dnamediatedassociationof pages 6-8) |
| Localization | Cac1 acts in the nucleus, particularly on nascent DNA at replication forks and at synthesis-dependent repair sites; its PCNA and DNA interactions stabilize fork association. | Functional interaction and fork-association evidence; strong | DNA-binding-defective and PCNA-binding-defective mutations show synergistic silencing and DNA-damage phenotypes. | Zhang et al., 2016 (zhang2016adnabinding pages 1-2) |
| Telomeric chromatin | Cac1 supports telomeric heterochromatin and normal Rap1 organization rather than serving only as a Rap1-specific localization factor. | Deletion genetics, reporter silencing, microscopy, and FISH; strong | Loss of RLF2/CAC1 causes reduced telomeric silencing, more numerous and diffuse Rap1 foci, and approximately 50% greater nuclear volume, while subtelomeric DNA positioning remains broadly normal. | Enomoto et al., 1997 (enomoto1997rlf2asubunit pages 1-2) |
| HM-locus silencing | CAF-1 primarily promotes maintenance, rather than de novo re-establishment, of silent mating-type chromatin. | Targeted genetic epistasis and silencing assays; strong | Reintroduced SIR3 restored HML silencing in cac1 sir3 cells but not in sir1 sir3 cells; sir1Δ cac1Δ abolished residual silencing maintained in most sir1Δ cells. | Enomoto & Berman, 1998 (enomoto1998chromatinassemblyfactor pages 11-12, enomoto1998chromatinassemblyfactor pages 1-2) |
| DNA-damage response | CAF-1 is dispensable for ordinary vegetative viability but contributes to chromatin restoration after DNA damage. | Null-mutant survival assays and domain mutagenesis; strong | Deleting any CAF-1 subunit increases UV sensitivity without a comparable increase in γ-ray sensitivity; WHD mutations also increase damage sensitivity. | Kaufman et al., 1997; Zhang et al., 2016 (kaufman1997ultravioletradiationsensitivity pages 6-7, zhang2016adnabinding pages 1-2) |
| Genome-stability pathway | Emerging evidence links Cac1/CAF-1 to suppression of replication-associated rDNA recombination and extrachromosomal rDNA-circle formation. | Direct budding-yeast genetics and molecular assays, initially reported as a 2024-posted preprint; moderate/emerging | cac1Δ produced approximately fourfold higher E-pro transcription; instability depended on Fob1 and Rad52 and was associated with increased DSB-end resection and altered nucleosome-coupled lagging-strand synthesis. | Futami et al., preprint posted 2024 and updated 2025 (futami2025thehistonechaperone pages 28-31) |
| Recent mechanistic update | Species warning: the 2024 experiments were performed in Schizosaccharomyces pombe, not Q12495-bearing S. cerevisiae. They support, but do not directly prove, a conserved dynamic CAF-1 model. | NMR, SAXS, modeling, in-vitro biochemistry, and in-vivo mutagenesis; strong for S. pombe, indirect for Cac1 | S. pombe CAF-1 is a 1:1:1 complex measured at 179 kDa; one H3–H4 dimer gives a 193-kDa complex. DNA binding to 40-bp duplexes had EC₅₀ = 0.7 ± 0.1 µM and Hill coefficient 2.7 ± 0.2. Pcf1 shares only 16% sequence identity with ScCac1. | Ouasti et al., 20 February 2024 (ouasti2024disorderedregionsand pages 7-9, ouasti2024disorderedregionsand pages 2-4, ouasti2024disorderedregionsand pages 4-5, ouasti2024disorderedregionsand pages 1-2) |
| Current application | RLF2/CAC1 is principally a research model for replication-coupled nucleosome assembly, epigenetic inheritance, heterochromatin maintenance, and repair-coupled genome stability; no established clinical or industrial application was identified. | Assessment of the gathered literature; well supported as a research use | Experimental applications include silencing reporters, CAF-1 reconstitution, histone-deposition assays, replication-fork studies, and DNA-damage genetics. | Zhang et al., 2016; Mattiroli et al., 2017; Ouasti et al., 2024 (zhang2016adnabinding pages 1-2, mattiroli2017dnamediatedassociationof pages 1-2, ouasti2024disorderedregionsand pages 1-2) |
Table: This table consolidates the strongest evidence for the identity, molecular function, mechanism, localization, pathways, and research uses of budding-yeast RLF2/CAC1. It also distinguishes direct Saccharomyces cerevisiae findings from the relevant but nonidentical 2024 Schizosaccharomyces pombe study.
The mandatory identity checks are satisfied:
The historical name “Rap1 localization factor 2” reflects the mutant phenotype through which RLF2 was identified; it should not be interpreted as making Cac1 a dedicated Rap1-transport or anchoring protein. Its primary function is CAF-1-mediated chromatin assembly.
CAF-1 is a histone chaperone rather than a catalyst. Cac1 supplies much of the complex’s interaction framework, while the assembled heterotrimer shields histone surfaces, engages nascent DNA, and promotes ordered histone transfer. No ATPase, transferase, nuclease, or other intrinsic catalytic activity has been demonstrated for Cac1. Its biologically relevant cargo is newly synthesized H3–H4, and its acceptor substrate is newly synthesized DNA or DNA undergoing repair-associated synthesis. (zhang2016adnabinding pages 1-2, mattiroli2017dnamediatedassociationof pages 1-2)
Detailed budding-yeast reconstitution established the following mechanism:
Thus, Cac1 does not merely bind histones. It implements a regulated handoff in which histone loading licenses DNA binding, two chaperone complexes cooperate, and DNA itself promotes histone release.
The C-terminal WHD is the best structurally resolved Cac1 element. Its 2.75-Å structure comprises four helices, two antiparallel β-strands, and a long wing loop. A basic surface containing Lys553, Lys560, Lys564, Lys568, Arg573, Lys577, Arg582, and Lys583 supports sequence-independent DNA binding. (zhang2016adnabinding pages 2-3)
Functional mutagenesis reinforces this assignment. The K564E/K568E WHD mutant retains H3–H4 binding but fails to form the histone-activated DNA-bound intermediate, separating histone recognition from productive deposition. More generally, DNA-binding-defective WHD mutations impair transcriptional silencing and increase DNA-damage sensitivity; combining them with PCNA-binding-defective Cac1 mutations worsens the phenotypes. DNA binding and PCNA engagement therefore cooperate to retain CAF-1 at active DNA-synthesis sites. (zhang2016adnabinding pages 1-2, mattiroli2017dnamediatedassociationof pages 6-8)
The supplied acidic CAF1A region is also mechanistically credible: budding-yeast experiments place an acidic regulatory segment within the histone-responsive interaction network, and the assembled histone-binding module includes Cac1 and Cac2. The exact boundaries used by InterPro/Pfam need not coincide perfectly with experimental truncations, but the functional assignments are concordant. (mattiroli2017dnamediatedassociationof pages 6-8)
Cac1 functions in the nucleus, on chromosomal DNA. Its most precise functional localization is transient rather than a fixed organelle compartment:
This is the primary pathway. PCNA encircles newly synthesized DNA and provides a platform for CAF-1 recruitment; Cac1’s DNA- and PCNA-binding activities cooperate with histone-triggered conformational switching. CAF-1 deposits H3–H4 tetramers, after which H2A–H2B addition can complete nucleosomes. (zhang2016adnabinding pages 1-2, mattiroli2017dnamediatedassociationof pages 16-17, mattiroli2017dnamediatedassociationof pages 1-2)
Deletion of CAC1, CAC2, or CAC3 does not prevent ordinary vegetative growth, showing that CAF-1 is nonessential under standard conditions. Nevertheless, each deletion increases UV sensitivity, and combining CAF-1-subunit mutations does not yield additive sensitivity, consistent with the three proteins acting in one complex. Comparable hypersensitivity to γ radiation was not observed in the original study. This pattern supports an important role in restoring chromatin during or after repair of UV lesions, while not implying exclusive action in nucleotide-excision repair. (kaufman1997ultravioletradiationsensitivity pages 6-7, kaufman1997ultravioletradiationsensitivity pages 1-2)
Loss of RLF2/CAC1 reduces repression of telomere-proximal reporters and alters the distribution of Rap1. Mutant nuclei contain more numerous and diffuse Rap1 foci and are approximately 50% larger. FISH showed that subtelomeric DNA distribution remained broadly similar to wild type, arguing that the Rap1 phenotype was not simply caused by wholesale telomere repositioning. Cac1 therefore supports a chromatin environment needed for normal telomeric protein organization and transcriptional silencing. (kaufman1997ultravioletradiationsensitivity pages 6-7, enomoto1997rlf2asubunit pages 1-2)
CAF-1 contributes mainly to maintenance of silencing at HML/HMR. In genetic re-establishment experiments, reintroducing SIR3 restored HML repression in cac1 sir3 cells but not in sir1 sir3 cells. Moreover, most sir1Δ cells retained residual repression, whereas sir1Δ cac1Δ cells lost it. These results support a model in which CAF-1-built nucleosomes stabilize inheritance of silent chromatin but are not absolutely required to nucleate silencing anew. (enomoto1998chromatinassemblyfactor pages 11-12, enomoto1998chromatinassemblyfactor pages 1-2)
A study first posted in 2024 and updated as a 2025 preprint directly links budding-yeast CAF-1 to ribosomal-DNA stability. CAF-1 deficiency increased chromosomal rDNA variation and extrachromosomal rDNA circles in pathways requiring the fork-block protein Fob1 and homologous-recombination factor Rad52. The work reported approximately fourfold greater E-pro transcription in cac1Δ, increased DSB-end resection, and reduced nucleosome-scale Okazaki-fragment signatures behind arrested forks. The proposed mechanism is that CAF-1-dependent H3–H4 deposition restricts excessive resection and misaligned Rad52-mediated repair among repetitive rDNA copies. Because the evidence was initially a preprint and postdates the requested 2023–2024 priority window in its analyzed form, it should be regarded as strong emerging evidence rather than part of the older consensus. (futami2025thehistonechaperone pages 49-50, futami2025thehistonechaperone pages 28-31)
Direct 2023–2024 mechanistic literature specifically centered on S. cerevisiae Cac1 is limited. The most relevant major 2024 structural study examined Schizosaccharomyces pombe CAF-1, not Q12495 and not S. cerevisiae. This distinction is essential.
Ouasti et al., version of record published 20 February 2024, reconstituted the fission-yeast Pcf1/Pcf2/Pcf3 complex and used NMR, SAXS, modeling, biochemistry, and in-vivo mutants. The measured complex was 179 kDa, close to the calculated 167-kDa 1:1:1 assembly; binding one H3–H4 dimer produced a 193-kDa complex. Up to approximately one-quarter of Pcf1 remained disordered in the assembled state. An acidic region folded upon histone binding, while the KER helix mediated DNA binding and enhanced association with PCNA. For 40-bp DNA, the reported EC₅₀ was 0.7 ± 0.1 µM with a Hill coefficient of 2.7 ± 0.2. DOI URL. (ouasti2024disorderedregionsand pages 7-9, ouasti2024disorderedregionsand pages 4-5, ouasti2024disorderedregionsand pages 1-2)
These results support a conserved model in which CAF-1 uses flexible/disordered regions and folded modules to integrate histone, DNA, and PCNA binding. They do not establish every detail for budding-yeast Cac1: Pcf1 shares only 16% sequence identity with ScCac1, and the fission-yeast WHD did not behave identically to the budding-yeast DNA-binding WHD. The 2024 work should therefore be treated as evolutionary and mechanistic support, not direct annotation evidence for individual Q12495 residues. (ouasti2024disorderedregionsand pages 7-9, ouasti2024disorderedregionsand pages 2-4)
RLF2/CAC1 currently has no established clinical, diagnostic, or industrial application. Its real-world use is as an experimental model for:
The strongest expert-level interpretation is that Cac1 is the central organizing subunit of a regulated deposition machine. Its phenotypes in silencing and DNA-damage resistance are downstream consequences of this primary chromatin-assembly role, not evidence for separate catalytic or signaling activities. The convergence of genetics, crystallography, quantitative stoichiometry, and reconstituted deposition makes this interpretation substantially stronger than annotations derived only from high-throughput screens. (zhang2016adnabinding pages 1-2, mattiroli2017dnamediatedassociationof pages 16-17, mattiroli2017dnamediatedassociationof pages 4-6)
Several boundaries should be retained in functional annotation:
References
(kaufman1997ultravioletradiationsensitivity pages 1-2): P. Kaufman, R. Kobayashi, and B. Stillman. Ultraviolet radiation sensitivity and reduction of telomeric silencing in saccharomyces cerevisiae cells lacking chromatin assembly factor-i. Genes & development, 11 3:345-57, Feb 1997. URL: https://doi.org/10.1101/gad.11.3.345, doi:10.1101/gad.11.3.345. This article has 473 citations and is from a highest quality peer-reviewed journal.
(enomoto1998chromatinassemblyfactor pages 1-2): Shinichiro Enomoto and Judith Berman. Chromatin assembly factor i contributes to the maintenance, but not the re-establishment, of silencing at the yeast silent mating loci. Genes & development, 12 2:219-32, Jan 1998. URL: https://doi.org/10.1101/gad.12.2.219, doi:10.1101/gad.12.2.219. This article has 258 citations and is from a highest quality peer-reviewed journal.
(enomoto1997rlf2asubunit pages 1-2): S. Enomoto, P. McCune-Zierath, M. Gerami‐Nejad, M. Sanders, and J. Berman. Rlf2, a subunit of yeast chromatin assembly factor-i, is required for telomeric chromatin function in vivo. Genes & development, 11 3:358-70, Feb 1997. URL: https://doi.org/10.1101/gad.11.3.358, doi:10.1101/gad.11.3.358. This article has 197 citations and is from a highest quality peer-reviewed journal.
(zhang2016adnabinding pages 1-2): Kuo Zhang, Yuan Gao, Jingjing Li, Rebecca Burgess, Junhong Han, Huanhuan Liang, Zhiguo Zhang, and Yingfang Liu. A dna binding winged helix domain in caf-1 functions with pcna to stabilize caf-1 at replication forks. Nucleic Acids Research, 44:5083-5094, Feb 2016. URL: https://doi.org/10.1093/nar/gkw106, doi:10.1093/nar/gkw106. This article has 71 citations and is from a highest quality peer-reviewed journal.
(mattiroli2017dnamediatedassociationof pages 1-2): Francesca Mattiroli, Yajie Gu, Tejas Yadav, Jeremy L Balsbaugh, Michael R Harris, Eileen S Findlay, Yang Liu, Catherine A Radebaugh, Laurie A Stargell, Natalie G Ahn, Iestyn Whitehouse, and Karolin Luger. Dna-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (caf-1) drives tetrasome assembly in the wake of dna replication. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.22799, doi:10.7554/elife.22799. This article has 111 citations and is from a domain leading peer-reviewed journal.
(mattiroli2017dnamediatedassociationof pages 4-6): Francesca Mattiroli, Yajie Gu, Tejas Yadav, Jeremy L Balsbaugh, Michael R Harris, Eileen S Findlay, Yang Liu, Catherine A Radebaugh, Laurie A Stargell, Natalie G Ahn, Iestyn Whitehouse, and Karolin Luger. Dna-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (caf-1) drives tetrasome assembly in the wake of dna replication. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.22799, doi:10.7554/elife.22799. This article has 111 citations and is from a domain leading peer-reviewed journal.
(kaufman1997ultravioletradiationsensitivity pages 5-6): P. Kaufman, R. Kobayashi, and B. Stillman. Ultraviolet radiation sensitivity and reduction of telomeric silencing in saccharomyces cerevisiae cells lacking chromatin assembly factor-i. Genes & development, 11 3:345-57, Feb 1997. URL: https://doi.org/10.1101/gad.11.3.345, doi:10.1101/gad.11.3.345. This article has 473 citations and is from a highest quality peer-reviewed journal.
(mattiroli2017dnamediatedassociationof pages 10-12): Francesca Mattiroli, Yajie Gu, Tejas Yadav, Jeremy L Balsbaugh, Michael R Harris, Eileen S Findlay, Yang Liu, Catherine A Radebaugh, Laurie A Stargell, Natalie G Ahn, Iestyn Whitehouse, and Karolin Luger. Dna-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (caf-1) drives tetrasome assembly in the wake of dna replication. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.22799, doi:10.7554/elife.22799. This article has 111 citations and is from a domain leading peer-reviewed journal.
(mattiroli2017dnamediatedassociationof pages 2-4): Francesca Mattiroli, Yajie Gu, Tejas Yadav, Jeremy L Balsbaugh, Michael R Harris, Eileen S Findlay, Yang Liu, Catherine A Radebaugh, Laurie A Stargell, Natalie G Ahn, Iestyn Whitehouse, and Karolin Luger. Dna-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (caf-1) drives tetrasome assembly in the wake of dna replication. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.22799, doi:10.7554/elife.22799. This article has 111 citations and is from a domain leading peer-reviewed journal.
(zhang2016adnabinding pages 2-3): Kuo Zhang, Yuan Gao, Jingjing Li, Rebecca Burgess, Junhong Han, Huanhuan Liang, Zhiguo Zhang, and Yingfang Liu. A dna binding winged helix domain in caf-1 functions with pcna to stabilize caf-1 at replication forks. Nucleic Acids Research, 44:5083-5094, Feb 2016. URL: https://doi.org/10.1093/nar/gkw106, doi:10.1093/nar/gkw106. This article has 71 citations and is from a highest quality peer-reviewed journal.
(mattiroli2017dnamediatedassociationof pages 6-8): Francesca Mattiroli, Yajie Gu, Tejas Yadav, Jeremy L Balsbaugh, Michael R Harris, Eileen S Findlay, Yang Liu, Catherine A Radebaugh, Laurie A Stargell, Natalie G Ahn, Iestyn Whitehouse, and Karolin Luger. Dna-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (caf-1) drives tetrasome assembly in the wake of dna replication. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.22799, doi:10.7554/elife.22799. This article has 111 citations and is from a domain leading peer-reviewed journal.
(enomoto1998chromatinassemblyfactor pages 11-12): Shinichiro Enomoto and Judith Berman. Chromatin assembly factor i contributes to the maintenance, but not the re-establishment, of silencing at the yeast silent mating loci. Genes & development, 12 2:219-32, Jan 1998. URL: https://doi.org/10.1101/gad.12.2.219, doi:10.1101/gad.12.2.219. This article has 258 citations and is from a highest quality peer-reviewed journal.
(kaufman1997ultravioletradiationsensitivity pages 6-7): P. Kaufman, R. Kobayashi, and B. Stillman. Ultraviolet radiation sensitivity and reduction of telomeric silencing in saccharomyces cerevisiae cells lacking chromatin assembly factor-i. Genes & development, 11 3:345-57, Feb 1997. URL: https://doi.org/10.1101/gad.11.3.345, doi:10.1101/gad.11.3.345. This article has 473 citations and is from a highest quality peer-reviewed journal.
(futami2025thehistonechaperone pages 28-31): Hajime Futami, Tsugumi Yamaji, Yuko Katayama, Nanase Arata, Takehiko Kobayashi, and Mariko Sasaki. The histone chaperone caf-1 prevents rad52-mediated instability of the budding yeast ribosomal dna during replication-coupled dna double-strand break repair. bioRxiv, Feb 2025. URL: https://doi.org/10.1101/2024.03.12.584701, doi:10.1101/2024.03.12.584701. This article has 0 citations.
(ouasti2024disorderedregionsand pages 7-9): Fouad Ouasti, Maxime Audin, Karine Fréon, Jean-Pierre Quivy, Mehdi Tachekort, Elizabeth Cesard, Aurélien Thureau, Virginie Ropars, Paloma Fernández Varela, Gwenaelle Moal, Ibrahim Soumana Adamou, Aleksandra Uryga, Pierre Legrand, Jessica Andreani, Raphaël Guerois, Geneviève Almouzni, Sarah Lambert, and Francoise Ochsenbein. Disordered regions and folded modules in caf-1 promote histone deposition in schizosaccharomyces pombe. eLife, Feb 2024. URL: https://doi.org/10.7554/elife.91461, doi:10.7554/elife.91461. This article has 6 citations and is from a domain leading peer-reviewed journal.
(ouasti2024disorderedregionsand pages 2-4): Fouad Ouasti, Maxime Audin, Karine Fréon, Jean-Pierre Quivy, Mehdi Tachekort, Elizabeth Cesard, Aurélien Thureau, Virginie Ropars, Paloma Fernández Varela, Gwenaelle Moal, Ibrahim Soumana Adamou, Aleksandra Uryga, Pierre Legrand, Jessica Andreani, Raphaël Guerois, Geneviève Almouzni, Sarah Lambert, and Francoise Ochsenbein. Disordered regions and folded modules in caf-1 promote histone deposition in schizosaccharomyces pombe. eLife, Feb 2024. URL: https://doi.org/10.7554/elife.91461, doi:10.7554/elife.91461. This article has 6 citations and is from a domain leading peer-reviewed journal.
(ouasti2024disorderedregionsand pages 4-5): Fouad Ouasti, Maxime Audin, Karine Fréon, Jean-Pierre Quivy, Mehdi Tachekort, Elizabeth Cesard, Aurélien Thureau, Virginie Ropars, Paloma Fernández Varela, Gwenaelle Moal, Ibrahim Soumana Adamou, Aleksandra Uryga, Pierre Legrand, Jessica Andreani, Raphaël Guerois, Geneviève Almouzni, Sarah Lambert, and Francoise Ochsenbein. Disordered regions and folded modules in caf-1 promote histone deposition in schizosaccharomyces pombe. eLife, Feb 2024. URL: https://doi.org/10.7554/elife.91461, doi:10.7554/elife.91461. This article has 6 citations and is from a domain leading peer-reviewed journal.
(ouasti2024disorderedregionsand pages 1-2): Fouad Ouasti, Maxime Audin, Karine Fréon, Jean-Pierre Quivy, Mehdi Tachekort, Elizabeth Cesard, Aurélien Thureau, Virginie Ropars, Paloma Fernández Varela, Gwenaelle Moal, Ibrahim Soumana Adamou, Aleksandra Uryga, Pierre Legrand, Jessica Andreani, Raphaël Guerois, Geneviève Almouzni, Sarah Lambert, and Francoise Ochsenbein. Disordered regions and folded modules in caf-1 promote histone deposition in schizosaccharomyces pombe. eLife, Feb 2024. URL: https://doi.org/10.7554/elife.91461, doi:10.7554/elife.91461. This article has 6 citations and is from a domain leading peer-reviewed journal.
(mattiroli2017dnamediatedassociationof pages 16-17): Francesca Mattiroli, Yajie Gu, Tejas Yadav, Jeremy L Balsbaugh, Michael R Harris, Eileen S Findlay, Yang Liu, Catherine A Radebaugh, Laurie A Stargell, Natalie G Ahn, Iestyn Whitehouse, and Karolin Luger. Dna-mediated association of two histone-bound complexes of yeast chromatin assembly factor-1 (caf-1) drives tetrasome assembly in the wake of dna replication. eLife, Mar 2017. URL: https://doi.org/10.7554/elife.22799, doi:10.7554/elife.22799. This article has 111 citations and is from a domain leading peer-reviewed journal.
(futami2025thehistonechaperone pages 49-50): Hajime Futami, Tsugumi Yamaji, Yuko Katayama, Nanase Arata, Takehiko Kobayashi, and Mariko Sasaki. The histone chaperone caf-1 prevents rad52-mediated instability of the budding yeast ribosomal dna during replication-coupled dna double-strand break repair. bioRxiv, Feb 2025. URL: https://doi.org/10.1101/2024.03.12.584701, doi:10.1101/2024.03.12.584701. This article has 0 citations.