Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing
Open accessAbstract
The histone chaperone Rtt106 binds histone H3 acetylated at lysine 56 (H3K56ac) and facilitates nucleosome assembly during several molecular processes. Both the structural basis of this modification-specific recognition and how this recognition informs Rtt106 function are presently unclear. Guided by our crystal structure of Rtt106, we identified two regions on its double-pleckstrin homology domain architecture that mediated histone binding. When histone binding was compromised, Rtt106 localized properly to chromatin but failed to deliver H3K56ac, leading to replication and silencing defects. By mutating analogous regions in the structurally homologous chromatin-reorganizer Pob3, we revealed a conserved histone-binding function for a basic patch found on both proteins. In contrast, a loop connecting two β-strands was required for histone binding by Rtt106 but was dispensable for Pob3 function. Unlike Rtt106, Pob3 histone binding was modification-independent, implicating the loop of Rtt106 in H3K56ac-specific recognition in vivo. Our studies described the structural origins of Rtt106 function, identified a conserved histone-binding surface, and defined a critical role for Rtt106:H3K56ac-binding specificity in silencing and replication-coupled nucleosome turnover.
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Loss of Rtt106 causes aberrant 'cryptic' transcription initiation within gene bodies and compromised silencing at the mating loci and telomeres, likely due to defective nucleosome assembly.
“Loss of Rtt106 causes aberrant ‘cryptic’ transcription initiation within gene bodies26 and compromised silencing at the mating loci and telomeres27,28, likely due to defective nucleosome assembly26,27,29.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [27]
The increased mRNA in rtt106Δ may reflect increased transcription initiation caused by defective histone deposition or increased nucleosome spacing.
“This may reflect increased transcription initiation that could be caused by defective histone deposition or increased nucleosome spacing in rtt106Δ26,27,29.”
From SWI/SNF and the histone chaperone Rtt106 drive expression of the Pleiotropic Drug Resistance network genes (2022) · cites this paper as [27]
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Regulation of Chromatin by FACT and NuA3
Chruscicki, A. (2014) · cIRcle (University of British Columbia) · doi:10.14288/1.0073776
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Faculty Opinions recommendation of Transcription shapes genome-wide histone acetylation patterns.
Mendoza, M. (2021) · Faculty Opinions – Post-Publication Peer Review of the Biomedical Literature · doi:10.3410/f.739339469.793584863
Faculty Opinions recommendation of Transcription shapes genome-wide histone acetylation patterns.
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Distinct DAXX effector modules separate H3.3 nucleosome assembly from ERV silencingPreprint
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- Authors
- Zunder, R. M., Antczak, A. J., Berger, J. M., & Rine, J.
- Affiliations
- QB3 (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2011-12-23
- Volume
- 109
- Issue
- 3
- Pages
- E144-53
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC3271894
- OpenAlex
- W2067533446
- Cited by
- 48
- References
- 56
- Citations by year
- 2026: 1 · 2024: 3 · 2023: 4 · 2022: 2 · 2021: 7 · 2020: 2 · 2019: 2 · 2018: 5 · 2017: 1 · 2016: 2 · 2015: 4 · 2014: 4 · 2013: 8 · 2012: 3
- FWCI
- 1.95
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Science Foundation
- National Cancer Institute (CA0777373)
- National Institute of General Medical Sciences (GM31105, R01GM031105, R37GM031105)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- histone chaperone, H3K56 acetylation, histone binding, chromatin silencing, DNA replication, nucleosome assembly, nucleosome turnover, chromatin reorganization, protein structure-function relationship
- MeSH terms
- Amino Acid Sequence, Chromatin, DNA Replication, Histones, Lysine, Models, Molecular, Molecular Sequence Data, Protein Binding, Saccharomyces cerevisiae, Surface Properties, Transcription Factors, Protein Structure, Tertiary, Molecular Chaperones, Gene Silencing, Saccharomyces cerevisiae Proteins, Histone Chaperones
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
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