The DOI matches its Crossref record; 64 of the 64 references it cites were found in a registry or an index.
Rtt106p is a histone chaperone involved in heterochromatin-mediated silencing
Open accessAbstract
Epigenetic inheritance of heterochromatin structure is an important cellular process whose mechanism remains elusive. In this article, we describe the identification of nine enhancers of the silencing defect of a Saccharomyces cerevisiae -PCNA mutant by screening a library of ≈4,700 viable yeast deletion mutants. Of the nine mutants identified, six ( hir1 , hir3 , sas2 , sas4 , sas5 , and sir1 ) were previously known to reduce silencing synergistically with a mutation in Cac1p, the large subunit of chromatin assembly factor 1 (CAF-1). The predicted gene products that are affected in three other mutants ( nam7 , msh2 , and rtt106 ) have not been implicated previously in silencing. Characterization of the rtt106 Δ allele revealed that it synergistically reduced heterochromatin silencing when combined with a mutation in Cac1p but not with a mutation in Asf1p (a histone H3 and H4 chaperone). Moreover, Rtt106p interacted with histones H3 and H4 both in vitro and in vivo , and it displayed a nucleosome assembly activity in vitro . Furthermore, Rtt106p interacts with CAF-1 physically through Cac1p. These biochemical and genetic data indicate that Rtt106p is a previously uncharacterized histone chaperone connecting S phase to epigenetic inheritance.
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“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 [28]
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Metadata
- Authors
- Huang, S., Zhou, H., Katzmann, D., Hochstrasser, M., Atanasova, E., & Zhang, Z.
- Affiliations
- Mayo Clinic (US)
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 2005-09-12
- Volume
- 102
- Issue
- 38
- Pages
- 13410-13415
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC1224646
- OpenAlex
- W2031481332
- Cited by
- 130
- References
- 64
- Citations by year
- 2026: 3 · 2025: 2 · 2024: 4 · 2023: 3 · 2022: 5 · 2021: 9 · 2020: 4 · 2019: 5 · 2018: 6 · 2017: 8 · 2016: 8 · 2015: 5 · 2014: 6 · 2013: 7 · 2012: 7
- FWCI
- 2.13
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Cancer Research UK
- University of Toronto
- National Institutes of Health
- National Institute of General Medical Sciences (R01GM046904, R37GM046904, GM-46904)
- 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 › Epigenetics and DNA Methylation
- Keywords
- histone chaperone, heterochromatin silencing, epigenetic inheritance, CAF-1, nucleosome assembly, histone H3, histone H4, S phase, Saccharomyces cerevisiae, Sir proteins
- MeSH terms
- Histones, Ribonucleases, Saccharomyces cerevisiae, Gene Expression Regulation, Fungal, S Phase, Gene Deletion, Proliferating Cell Nuclear Antigen, Molecular Chaperones, Gene Silencing, Saccharomyces cerevisiae Proteins, Chromatin Assembly and Disassembly, Epigenesis, Genetic
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