SIR3 Antibody

1. Yeast Sir2 and Sir3 heterochromatin proteins directly modify the local chromatin environment of euchromatic DNA replication origins. PMID: 29795547
2. Here, the authors analyze binding of the Sir proteins to reconstituted mono-, di-, tri-, and tetra-nucleosomal chromatin templates and show that key Sir-Sir interactions bridge only sites on different nucleosomes but not sites on the same nucleosome, and are therefore 'interrupted' with respect to sites on the same nucleosome. PMID: 27835568
3. Repair of UV-induced DNA lesions in Saccharomyces cerevisiae telomeres is moderated by Sir2 and Sir3, and inhibited by yKu-Sir4 interaction. PMID: 28334768
4. silencing requires Sir2, a highly-conserved NAD(+)-dependent histone deacetylase. At locations other than the rDNA, silencing also requires additional Sir proteins, Sir1, Sir3, and Sir4 that together form a repressive heterochromatin-like structure termed silent chromatin. PMID: 27516616
5. results suggest that Sir3 exhibits novel binding parameters and gene regulatory functions at the CN binding domains. PMID: 26957548
6. Sir3 interacts with nucleosomal arrays with a stoichiometry of two Sir3 monomers per nucleosome. We also find that Sir3 fibres are less compact than canonical magnesium-induced 30 nm fibres. PMID: 25163529
7. Direct interactions promote eviction of the Sir3 heterochromatin protein by the SWI/SNF chromatin remodeling enzyme. PMID: 25453095
8. Telomere clusters, their dynamics, and their nuclear distribution result from random motion, aggregation, and dissociation of telomeric regions, specifically determined by the amount of Sir3. PMID: 23576549
9. The crystal structure of the N-terminally acetylated BAH domain of Sir3 bound to the nucleosome core particle reveals that the N-terminal acetylation stabilizes the interaction of Sir3 with the nucleosome. PMID: 23934150
10. By X-ray crystallography, we show that the acetylated N terminus of Sir3 does not interact with the nucleosome directly. Instead, it stabilizes a nucleosome-binding loop in the BAH domain. PMID: 23934152
11. Sir3 binding generates a more stable nucleosome by clamping H4R17 and R19 to nucleosomal DNA, and raise the possibility that such induced changes in histone-DNA contacts play major roles in the regulation of chromatin structure. PMID: 23650358
12. Dimerization of Sir3 via its C-terminal winged helix domain is essential for yeast heterochromatin formation. PMID: 23299941
13. examined gene expression and molecular markers of silencing at the silent mating type loci under conditions of limiting Sir3 protein PMID: 22586263
14. crystal structure of complex of Sir3 BAH domain and nucleosome core particle at 3.0 A resolution; structure explains how covalent modifications on H4K16 and H3K79 regulate formation of silencing complex containing the nucleosome as a central component PMID: 22096199
15. Sir3 promotes telomere clustering independently of silencing in yeast PMID: 21300849
16. Genome-wide nucleosome mapping revealed that Sir3 binding to subtelomeric regions was associated with overpackaging of subtelomeric promoters. PMID: 21336256
17. Data suggest that histone H3 Lys-4 methylation prevents Sir3p association at euchromatic sites and therefore concentrates Sir3p at unmodified, heterochromatic regions of the genome. PMID: 15280381
18. sir2 and sir4, but not sir3, have roles in silencing of DNA breakage and recombination PMID: 15647382
19. The structure and function of the Sir3 BAH domain have been established. PMID: 16581798
20. These findings imply that the Sir3p-BAH domain structure has evolved for functions distinct from those of the Orc1p-BAH domain. PMID: 16641491
21. Sir3-Sir4 complexes form progressively higher order assemblies with increasing protein concentration, with implications for the mechanism of gene silencing. PMID: 16717101
22. Chromatin immunoprecipitation analyses of wild-type and ctd-Y964A mutant cells indicate an association of the C-terminal domain with the deacetylated histone tails of H3 and H4 that is necessary for the recruitment of Sir3 PMID: 16908543
23. Analysis of full-length recombinant Sir3p domain organization and quaternary structure supports a nucleosome bridging model for Sir3p-dependent regulation of chromatin architecture. PMID: 17176117
24. Results show that the BAH domain of Sir3 is a nucleosome- and histone-tail-binding domain and its binding to nucleosomes is regulated by the N terminus residues of histone H4 and the globular domain of histone H3 on the exposed surface of the nucleosome. PMID: 18158899
25. These results define how SIR3p may function as a chromatin architectural protein and provide new insight into the interplay between endogenous and protein-mediated chromatin fiber condensation pathways. PMID: 18362167
26. BAH domain of Sir3 binds to histone H3K79; acetylation of the BAH domain is required for the binding specificity of Sir3 for nucleosomes unmethylated at H3K79. PMID: 18391024
27. Results underscore the importance of proper interactions between Sir3 and the nucleosome in silent chromatin assembly. PMID: 18794362
28. Sir3p BAH domain directly binds the nucleosomal LRS domain. PMID: 19079580
29. Role of nucleic acid binding in Sir3-dependent interactions with chromatin fibers is reported. PMID: 19099415
30. The functional specialization of Sir3,as a silencing protein was facilitated by the tandem duplication of the OIR domain in the Sir1 family, allowing distinct Sir1-Sir3 and Sir1-Orc1 interactions through OIR-BAH domain interactions. PMID: 19171939
31. These results, together with the previously characterized interaction between the C-terminal region of Sir3 and the histone H3/H4 tails, suggest that Sir3 utilizes multiple domains to interact with nucleosomes. PMID: 19273586

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KEGG: sce:YLR442C

STRING: 4932.YLR442C