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this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
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The literature synthesized here refers specifically to S. cerevisiae Rpd3 (gene RPD3, ORF YNL330C), a class I histone deacetylase (HDAC) that is the catalytic subunit of Sin3-associated HDAC complexes Rpd3L and Rpd3S. Multiple 2023–2024 structural studies explicitly describe “Rpd3 from the budding yeast Saccharomyces cerevisiae” as a class I HDAC functioning in these two complexes, matching the UniProt description for P32561. (carrozza2024rpd3smeetsthe pages 1-2, patel2023cryoemstructureof pages 1-2)
Rpd3 is a class I HDAC and is described as the founding member of class I HDACs in yeast. (zhang2023structuralbasisfor pages 1-2)
Mechanistically, its catalytic site is Zn²⁺-dependent: a 2023 Rpd3S–nucleosome cryo-EM structure describes a catalytic Zn²⁺ coordinated/stabilized by D186, H188, and D274 in Rpd3. (zhang2023structuralbasisfor pages 1-2)
Definition (HDAC reaction): Rpd3-containing complexes remove acetyl groups from ε-N-acetyl-lysine residues on histone tails (lysine deacetylation), modulating chromatin accessibility and transcriptional output. Functionally, the enzyme acts primarily as part of Rpd3L (large) or Rpd3S (small) complexes rather than as a solitary enzyme. (patel2023cryoemstructureof pages 1-2, carrozza2024rpd3smeetsthe pages 1-2)
A central organizing principle is that Rpd3 forms two distinct Sin3-associated complexes that target different genomic regions:
The 2024 expert commentary emphasizes the division of labor: Rpd3L is promoter-associated and Rpd3S acts behind elongating RNA polymerase II to maintain gene-body chromatin in a deacetylated state. (carrozza2024rpd3smeetsthe pages 1-2)
The period 2023–2024 saw a major leap in mechanistic understanding through multiple cryo-EM structures of Rpd3 complexes on nucleosomal substrates.
Rpd3S is recruited to H3K36-methylated nucleosomes and suppresses cryptic initiation. A 2023 Nature study solved cryo-EM structures of Rpd3S free and nucleosome-bound, describing an architecture with two Eaf3–Rco1 heterodimers assembled asymmetrically around the catalytic core (Rpd3 + Sin3) and demonstrating multivalent recognition of H3K36me3 and DNA to position the Rpd3 catalytic center for deacetylation. (guan2023diversemodesof pages 1-2, guan2023diversemodesof pages 2-3)
A complementary 2023 Cell Research cryo-EM structure of the Rpd3S holoenzyme bound to a nucleosome (3.7 Å) captured an intact H3 tail threaded into the active site with H3K18 poised for catalysis and reported in vitro deacetylation of H3K18ac. (zhang2023structuralbasisfor pages 1-2)
Another 2023 study reported a structure of Rpd3S bound to nucleosome (3.1 Å, as described in the publication metadata; mechanistic details in the text include Eaf3 recognition of H3K36me3 via an aromatic cage) and noted that Rpd3S engages chromatin multivalently, helping explain how the complex acts cotranscriptionally on gene bodies. (li2023structureofhistone pages 4-5)
A 2023 Nature Communications study solved the cryo-EM structure of the 12-subunit Rpd3L complex (~3.5 Å). It showed Rpd3 is the sole catalytic subunit and that the complex is organized as an asymmetric dimer in which two copies each of Sin3, Rpd3, and Ume1 form two lobes. Importantly, it found that the active site of one Rpd3 is occluded by a leucine from Rxt2, indicating complex-mediated regulation of catalytic accessibility. (patel2023cryoemstructureof pages 1-2)
A 2024 Cell Research commentary (Carrozza & Workman) integrated multiple 2023 structural results, emphasizing how reader modules and nucleosome geometry determine where Rpd3S acts and which histone tails are engaged. It highlights that Rpd3S can engage/deacetylate H3 tail residues spanning K9 to K18, and reports differential apparent efficiencies at different H3 lysines in biochemical assays (e.g., more efficient deacetylation at H3K23/H3K14 than H3K9/H3K18/H3K27 at lower enzyme amounts). (carrozza2024rpd3smeetsthe pages 2-2)
Recent biochemical assays and structural states support that Rpd3S can act on multiple histone tail acetylation sites:
Structural evidence indicates context-dependent catalytic engagement:
Thus, current understanding is that Rpd3S has broad histone-tail deacetylation capability, with chromatin context and binding mode determining whether H3- or H4-tail lysines are preferentially presented to the active site. (guan2023diversemodesof pages 2-3, zhang2023structuralbasisfor pages 1-2)
A key modern insight is that Rpd3’s specificity in vivo is achieved by non-catalytic subunits that read histone methyl marks and DNA geometry.
H3K36me3 readout (Eaf3 chromodomain):
* Rpd3S is recruited to gene bodies via Set2-dependent H3K36 methylation; Eaf3’s chromodomain recognizes H3K36me2/3. (carrozza2024rpd3smeetsthe pages 1-2, yague‐sanz2024shapingthechromatin pages 5-6)
* A 2023 Nature study describes H3K36me3 recognition via an Eaf3 aromatic cage comprising Y23, Y81, W84, W88. (guan2023diversemodesof pages 2-3)
H3K4me0 readout (Rco1 PHD1):
* Rco1 PHD1 recognizes unmodified H3K4, and methylation destabilizes binding, helping restrict Rpd3S activity to coding regions (which tend to be H3K4 hypomethylated relative to promoters). (zhang2023structuralbasisfor pages 1-2)
* The 2023 Nature study measured Kd ≈ 39 μM for PHD1 binding H3(1–10). (guan2023diversemodesof pages 2-3)
DNA contacts and nucleosome geometry:
Rpd3S engages nucleosomes through multiple DNA interfaces involving Sin3 and reader modules, anchoring the complex and orienting it so histone tails can be threaded into the active site. (zhang2023structuralbasisfor pages 1-2, guan2023diversemodesof pages 2-3)
Rpd3S comprises the core catalytic and scaffold components plus chromatin-binding subunits:
A 2023 report on the complete Rpd3S–nucleosome assembly describes a nucleosome-bound complex with 1× Sin3, 1× Rpd3, 1× Ume1, and 2× each of Eaf3 and Rco1. (markert2023structureofthea pages 1-2)
Rpd3L is a larger promoter-associated complex; a 2023 cryo-EM study describes it as a 12-subunit complex where Sin3 serves as principal scaffold integrating the sole catalytic subunit Rpd3 and multiple structural subunits (including, among others, Rxt2, Pho23, Rxt3, Sap30, Sds3, Dep1). (patel2023cryoemstructureof pages 1-2)
Rpd3S is targeted to transcribed regions and functions to suppress cryptic/spurious intragenic transcription initiation, restoring deacetylated chromatin behind elongating RNA polymerase II. (carrozza2024rpd3smeetsthe pages 1-2)
The mechanistic model is: Set2 deposits H3K36me3 during elongation → Eaf3 reads H3K36me3 → Rpd3S is recruited and oriented on nucleosomes → deacetylation of H3/H4 tails reduces inappropriate initiation within ORFs. (yague‐sanz2024shapingthechromatin pages 5-6, guan2023diversemodesof pages 2-3)
Rpd3L is described as acting primarily at promoters, performing localized deacetylation near recruitment sites of DNA-binding factors. (patel2023cryoemstructureof pages 1-2)
A yeast review notes Rpd3L recruitment can involve association with sequence-specific factors and/or interactions with promoter marks such as H3K4me3, whereas Rpd3S is recruited via H3K36 methylation in gene bodies. (yague‐sanz2024shapingthechromatin pages 5-6)
Rpd3 is repeatedly framed as a prototypical/founding class I HDAC, enabling yeast to serve as a tractable model to study complex-level HDAC regulation that is conserved across eukaryotes. (zhang2023structuralbasisfor pages 1-2, patel2023cryoemstructureof pages 1-2)
A key “real-world implementation” of the yeast system is using purified native complexes to test inhibitors and understand accessibility/complex-specific regulation:
Key reported quantitative details useful for functional annotation include:
The overall architecture of Rpd3S bound to an H3K36me3 nucleosome—including labeled subunits (Sin3, Rpd3, Eaf3, Rco1) and the nucleosome—is illustrated in a cryo-EM figure from Guan et al. 2023. (guan2023diversemodesof media 4647e40e)
| Aspect | Current understanding | Key supporting 2023–2024 sources (with DOI/URL) | Notes/quantitative details |
|---|---|---|---|
| Enzyme class / reaction | Rpd3 (UniProt P32561; YNL330C) is the budding yeast founding class I, Zn²⁺-dependent histone deacetylase that catalyzes hydrolytic removal of ε-N-acetyl groups from lysine residues on histones, functioning as the catalytic subunit of Sin3-associated HDAC complexes. It acts in both Rpd3S and Rpd3L chromatin complexes rather than as a free enzyme. (guan2023diversemodesof pages 1-2, patel2023cryoemstructureof pages 1-2, zhang2023structuralbasisfor pages 1-2) | Guan et al., 2023, Nature. DOI: 10.1038/s41586-023-06349-1. https://doi.org/10.1038/s41586-023-06349-1 (guan2023diversemodesof pages 1-2); Patel et al., 2023, Nat Commun. DOI: 10.1038/s41467-023-38687-z. https://doi.org/10.1038/s41467-023-38687-z (patel2023cryoemstructureof pages 1-2); Zhang et al., 2023, Cell Research. DOI: 10.1038/s41422-023-00884-2. https://doi.org/10.1038/s41422-023-00884-2 (zhang2023structuralbasisfor pages 1-2) | Active-site Zn²⁺ is structurally stabilized/coordinated by D186, H188, D274 in the 2023 Rpd3S cryo-EM study. Rpd3L is ~1.2 MDa; Rpd3S is ~0.6 MDa. (zhang2023structuralbasisfor pages 1-2) |
| Rpd3S complex composition / stoichiometry / targeting logic | Rpd3S is the gene-body HDAC complex specialized for transcribed chromatin. Core composition: Rpd3, Sin3, Ume1 plus chromatin-targeting subunits Eaf3 and Rco1. Recent structures show a stoichiometry of 1× Rpd3, 1× Sin3, 1× Ume1, 2× Eaf3, 2× Rco1 in the nucleosome-bound assembly. Recruitment/targeting is driven by multivalent readout of H3K36me3 and H3K4me0 together with nucleosomal/linker DNA contacts. Eaf3 chromodomain reads H3K36 methylation, while Rco1 PHD1 prefers unmodified H3K4, helping bias Rpd3S toward coding regions. (markert2023structureofthea pages 1-2, guan2023diversemodesof pages 1-2, zhang2023structuralbasisfor pages 1-2, guan2023diversemodesof pages 2-3) | Markert et al., 2023, Nat Commun. DOI: 10.1038/s41467-023-43968-8. https://doi.org/10.1038/s41467-023-43968-8 (markert2023structureofthea pages 1-2); Guan et al., 2023. DOI: 10.1038/s41586-023-06349-1. https://doi.org/10.1038/s41586-023-06349-1 (guan2023diversemodesof pages 1-2); Zhang et al., 2023. DOI: 10.1038/s41422-023-00884-2. https://doi.org/10.1038/s41422-023-00884-2 (zhang2023structuralbasisfor pages 1-2); Li et al., 2023, Nat Struct Mol Biol. DOI: 10.1038/s41594-023-01121-5. https://doi.org/10.1038/s41594-023-01121-5 (li2023structureofhistone pages 4-5) | Eaf3 CHD aromatic cage residues recognizing H3K36me3: Y23, Y81, W84, W88. Rco1 PHD1 binds H3(1–10) with Kd ≈ 39 μM and is destabilized by H3K4 methylation. The Sin3 scaffold and Rco1/Eaf3 also contact linker/nucleosomal DNA, enabling orientation over the nucleosome. (li2023structureofhistone pages 4-5, guan2023diversemodesof pages 2-3, zhang2023structuralbasisfor pages 1-2) |
| Rpd3L complex composition / promoter targeting | Rpd3L is the larger promoter-proximal Sin3-associated deacetylase complex that performs localized deacetylation at or near recruitment sites of DNA-binding factors. It shares the catalytic/scaffold core (Rpd3, Sin3, Ume1) with Rpd3S but contains Rpd3L-specific accessory subunits such as Pho23, Rxt2, Rxt3, Sap30, Sds3, Dep1 (and related promoter-recruitment factors noted in recent literature). Rpd3L is targeted primarily to promoters, often via transcription factors and/or promoter chromatin marks including H3K4me3 readout by Pho23-linked mechanisms. (patel2023cryoemstructureof pages 1-2, carrozza2024rpd3smeetsthe pages 1-2, dong2023structuralbasisof pages 1-2, yague‐sanz2024shapingthechromatin pages 5-6) | Patel et al., 2023. DOI: 10.1038/s41467-023-38687-z. https://doi.org/10.1038/s41467-023-38687-z (patel2023cryoemstructureof pages 1-2); Carrozza & Workman, 2024, Cell Research. DOI: 10.1038/s41422-023-00899-9. https://doi.org/10.1038/s41422-023-00899-9 (carrozza2024rpd3smeetsthe pages 1-2); Dong et al., 2023, Cell Research. DOI: 10.1038/s41422-023-00869-1. https://doi.org/10.1038/s41422-023-00869-1 (dong2023structuralbasisof pages 1-2); Yague-Sanz, 2024, Yeast. DOI: 10.1002/yea.3921. https://doi.org/10.1002/yea.3921 (yague‐sanz2024shapingthechromatin pages 5-6) | Structural work indicates an asymmetric dimeric Rpd3L architecture with two copies each of Rpd3, Sin3, and Ume1 in the core of the 12-subunit complex; one Rpd3 active site can be occluded by Rxt2, suggesting regulated catalytic access. (patel2023cryoemstructureof pages 1-2) |
| Known / assayed histone substrate sites and preferences | Recent structural/biochemical studies show that Rpd3S deacetylates multiple acetyl-lysine sites on H3 and H4 tails. Assayed H3 sites include H3K9ac, H3K14ac, H3K18ac, H3K23ac, H3K27ac; assayed H4 sites include H4K5ac, H4K8ac, H4K12ac, H4K16ac. Distinct catalytic states suggest context-dependent substrate use: some structures position Rpd3S for H4-tail deacetylation, whereas others capture an H3-tail entering the active site with H3K18 poised for catalysis. (zhang2023structuralbasisfor pages 1-2, carrozza2024rpd3smeetsthe pages 2-2, guan2023diversemodesof pages 5-6) | Zhang et al., 2023. DOI: 10.1038/s41422-023-00884-2. https://doi.org/10.1038/s41422-023-00884-2 (zhang2023structuralbasisfor pages 1-2); Guan et al., 2023. DOI: 10.1038/s41586-023-06349-1. https://doi.org/10.1038/s41586-023-06349-1 (guan2023diversemodesof pages 5-6); Carrozza & Workman, 2024. DOI: 10.1038/s41422-023-00899-9. https://doi.org/10.1038/s41422-023-00899-9 (carrozza2024rpd3smeetsthe pages 2-2); Dong et al., 2023. DOI: 10.1038/s41422-023-00869-1. https://doi.org/10.1038/s41422-023-00869-1 (dong2023structuralbasisof pages 1-2) | In one cryo-EM state, H3K18 is oriented toward catalytic Zn²⁺; H3K9/H3K14 were not accommodated in that exact conformation, showing substrate-state dependence. Commentary summarizing biochemical assays notes lower enzyme amounts deacetylated H3K23/H3K14 more efficiently than H3K9/H3K18/H3K27. Recent structures also indicate Rpd3S can sample multiple tails and catalytic modes. (zhang2023structuralbasisfor pages 1-2, carrozza2024rpd3smeetsthe pages 2-2, dong2023structuralbasisof pages 1-2) |
| Mechanistic / structural highlights | 2023 cryo-EM studies transformed understanding of Rpd3 by revealing how noncatalytic subunits specify chromatin engagement. Sin3 wraps around catalytic Rpd3 and contributes key DNA-binding surfaces; Eaf3 and Rco1 form duplicated reader modules that contact histone marks and DNA. Rpd3S can adopt multiple nucleosome-binding states (“close,” “loose,” alternative deacetylation, linker-tightening), explaining how the enzyme reaches different histone tails and even engages neighboring nucleosomes. (zhang2023structuralbasisfor pages 1-2, li2023structureofhistone pages 4-5, guan2023diversemodesof pages 2-3, guan2023diversemodesof media 4647e40e) | Zhang et al., 2023. DOI: 10.1038/s41422-023-00884-2. https://doi.org/10.1038/s41422-023-00884-2 (zhang2023structuralbasisfor pages 1-2); Li et al., 2023. DOI: 10.1038/s41594-023-01121-5. https://doi.org/10.1038/s41594-023-01121-5 (li2023structureofhistone pages 4-5); Guan et al., 2023. DOI: 10.1038/s41586-023-06349-1. https://doi.org/10.1038/s41586-023-06349-1 (guan2023diversemodesof pages 2-3); Figure/context summary from Guan et al. overall model (guan2023diversemodesof media 4647e40e) | Structural details include: 3.7 Å Rpd3S–nucleosome structure (zhang2023structuralbasisfor pages 1-2); 3.5 Å alternative Rpd3S structures including linker-tightening states (dong2023structuralbasisof pages 1-2); 3.1 Å nucleosome-bound structure in another study (li2023structureofhistone pages 4-5). Eaf3 CHD makes aromatic-cage recognition of H3K36me3, while Rco1 PHD1 enforces H3K4me0 preference; Sin3 basic surfaces anchor DNA. (zhang2023structuralbasisfor pages 1-2, li2023structureofhistone pages 4-5, guan2023diversemodesof pages 2-3) |
| Cellular localization on chromatin / biological role | Functional division of labor is now clear: Rpd3S acts mainly across transcribed gene bodies, where it is recruited cotranscriptionally via Set2-linked H3K36me3 and associated with elongating RNAPII to restore a deacetylated chromatin state and suppress cryptic/spurious intragenic transcription. Rpd3L acts mainly at promoters, where it mediates localized repression or fine-tuning near recruitment sites of transcription factors and promoter marks. (carrozza2024rpd3smeetsthe pages 1-2, dong2023structuralbasisof pages 1-2, yague‐sanz2024shapingthechromatin pages 5-6) | Carrozza & Workman, 2024. DOI: 10.1038/s41422-023-00899-9. https://doi.org/10.1038/s41422-023-00899-9 (carrozza2024rpd3smeetsthe pages 1-2); Dong et al., 2023. DOI: 10.1038/s41422-023-00869-1. https://doi.org/10.1038/s41422-023-00869-1 (dong2023structuralbasisof pages 1-2); Yague-Sanz, 2024. DOI: 10.1002/yea.3921. https://doi.org/10.1002/yea.3921 (yague‐sanz2024shapingthechromatin pages 5-6) | Gene-body acetylation accumulates when Rpd3S is lost, consistent with its elongation-coupled deacetylase role. Rpd3S also shows possible di-nucleosome preference and linker-length dependence in recent work, supporting action on chromatin behind RNAPII rather than isolated peptides. (guan2023diversemodesof pages 1-2, carrozza2024rpd3smeetsthe pages 2-2) |
Table: This table summarizes the current functional annotation of Saccharomyces cerevisiae Rpd3 (UniProt P32561), emphasizing 2023–2024 structural and mechanistic advances. It highlights catalytic activity, Rpd3S/Rpd3L complex biology, substrate specificity, chromatin localization, and key quantitative details useful for annotation.
Key 2023–2024 sources used heavily in this report:
References
(carrozza2024rpd3smeetsthe pages 1-2): Michael J. Carrozza and Jerry L. Workman. Rpd3s meets the nucleosome. Cell research, 34:1-2, Nov 2024. URL: https://doi.org/10.1038/s41422-023-00899-9, doi:10.1038/s41422-023-00899-9. This article has 2 citations and is from a domain leading peer-reviewed journal.
(patel2023cryoemstructureof pages 1-2): Avinash B. Patel, Jinkang Qing, Kelly H. Tam, Sara Zaman, Maria Luiso, Ishwar Radhakrishnan, and Yuan He. Cryo-em structure of the saccharomyces cerevisiae rpd3l histone deacetylase complex. Nature Communications, May 2023. URL: https://doi.org/10.1038/s41467-023-38687-z, doi:10.1038/s41467-023-38687-z. This article has 20 citations and is from a highest quality peer-reviewed journal.
(zhang2023structuralbasisfor pages 1-2): Yueyue Zhang, Mengxue Xu, Po Wang, Jiahui Zhou, Guangxian Wang, Shuailong Han, Gang Cai, and Xuejuan Wang. Structural basis for nucleosome binding and catalysis by the yeast rpd3s/hdac holoenzyme. Cell Research, 33:971-974, Oct 2023. URL: https://doi.org/10.1038/s41422-023-00884-2, doi:10.1038/s41422-023-00884-2. This article has 12 citations and is from a domain leading peer-reviewed journal.
(guan2023diversemodesof pages 1-2): Haipeng Guan, Pei Wang, Pei Zhang, Chun Ruan, Yutian Ou, Bo Peng, Xiangdong Zheng, Jianlin Lei, Bing Li, Chuangye Yan, and Haitao Li. Diverse modes of h3k36me3-guided nucleosomal deacetylation by rpd3s. Nature, 620:669-675, Jul 2023. URL: https://doi.org/10.1038/s41586-023-06349-1, doi:10.1038/s41586-023-06349-1. This article has 40 citations and is from a highest quality peer-reviewed journal.
(guan2023diversemodesof pages 2-3): Haipeng Guan, Pei Wang, Pei Zhang, Chun Ruan, Yutian Ou, Bo Peng, Xiangdong Zheng, Jianlin Lei, Bing Li, Chuangye Yan, and Haitao Li. Diverse modes of h3k36me3-guided nucleosomal deacetylation by rpd3s. Nature, 620:669-675, Jul 2023. URL: https://doi.org/10.1038/s41586-023-06349-1, doi:10.1038/s41586-023-06349-1. This article has 40 citations and is from a highest quality peer-reviewed journal.
(li2023structureofhistone pages 4-5): Wulong Li, Hengjun Cui, Zhimin Lu, and Haibo Wang. Structure of histone deacetylase complex rpd3s bound to nucleosome. Nature structural & molecular biology, 30:1893-1901, Oct 2023. URL: https://doi.org/10.1038/s41594-023-01121-5, doi:10.1038/s41594-023-01121-5. This article has 18 citations and is from a highest quality peer-reviewed journal.
(carrozza2024rpd3smeetsthe pages 2-2): Michael J. Carrozza and Jerry L. Workman. Rpd3s meets the nucleosome. Cell research, 34:1-2, Nov 2024. URL: https://doi.org/10.1038/s41422-023-00899-9, doi:10.1038/s41422-023-00899-9. This article has 2 citations and is from a domain leading peer-reviewed journal.
(guan2023diversemodesof pages 5-6): Haipeng Guan, Pei Wang, Pei Zhang, Chun Ruan, Yutian Ou, Bo Peng, Xiangdong Zheng, Jianlin Lei, Bing Li, Chuangye Yan, and Haitao Li. Diverse modes of h3k36me3-guided nucleosomal deacetylation by rpd3s. Nature, 620:669-675, Jul 2023. URL: https://doi.org/10.1038/s41586-023-06349-1, doi:10.1038/s41586-023-06349-1. This article has 40 citations and is from a highest quality peer-reviewed journal.
(yague‐sanz2024shapingthechromatin pages 5-6): Carlo Yague‐Sanz. Shaping the chromatin landscape at rrna and trna genes, an emerging new role for rna polymerase ii transcription? Yeast, 41:135-147, Dec 2024. URL: https://doi.org/10.1002/yea.3921, doi:10.1002/yea.3921. This article has 7 citations and is from a peer-reviewed journal.
(markert2023structureofthea pages 1-2): Jonathan W. Markert, Seychelle M. Vos, and Lucas Farnung. Structure of the complete s. cerevisiae rpd3s-nucleosome complex. bioRxiv, Aug 2023. URL: https://doi.org/10.1101/2023.08.03.551877, doi:10.1101/2023.08.03.551877. This article has 6 citations.
(guan2023diversemodesof media 4647e40e): Haipeng Guan, Pei Wang, Pei Zhang, Chun Ruan, Yutian Ou, Bo Peng, Xiangdong Zheng, Jianlin Lei, Bing Li, Chuangye Yan, and Haitao Li. Diverse modes of h3k36me3-guided nucleosomal deacetylation by rpd3s. Nature, 620:669-675, Jul 2023. URL: https://doi.org/10.1038/s41586-023-06349-1, doi:10.1038/s41586-023-06349-1. This article has 40 citations and is from a highest quality peer-reviewed journal.
(dong2023structuralbasisof pages 1-2): Shuqi Dong, Huadong Li, Meilin Wang, Nadia Rasheed, Binqian Zou, Xijie Gao, Jiali Guan, Weijie Li, Jiale Zhang, Chi Wang, Ningkun Zhou, Xue Shi, Mei Li, Min Zhou, Junfeng Huang, He Li, Ying Zhang, Koon Ho Wong, Xiaofei Zhang, William Chong Hang Chao, and Jun He. Structural basis of nucleosome deacetylation and dna linker tightening by rpd3s histone deacetylase complex. Cell Research, 33:790-801, Sep 2023. URL: https://doi.org/10.1038/s41422-023-00869-1, doi:10.1038/s41422-023-00869-1. This article has 12 citations and is from a domain leading peer-reviewed journal.