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  4. Recombinant Saccharomyces cerevisiae Regulatory protein SIR3 (SIR3), partial

Recombinant Saccharomyces cerevisiae Regulatory protein SIR3 (SIR3), partial

  • 中文名称：
    酿酒酵母SIR3重组蛋白
  • 货号：
    CSB-YP356918SVG
  • 规格：
  • 来源：
    Yeast
  • 其他：
  • 中文名称：
    酿酒酵母SIR3重组蛋白
  • 货号：
    CSB-EP356918SVG
  • 规格：
  • 来源：
    E.coli
  • 其他：
  • 中文名称：
    酿酒酵母SIR3重组蛋白
  • 货号：
    CSB-EP356918SVG-B
  • 规格：
  • 来源：
    E.coli
  • 共轭：
    Avi-tag Biotinylated

    E. coli biotin ligase (BirA) is highly specific in covalently attaching biotin to the 15 amino acid AviTag peptide. This recombinant protein was biotinylated in vivo by AviTag-BirA technology, which method is BriA catalyzes amide linkage between the biotin and the specific lysine of the AviTag.

  • 其他：
  • 中文名称：
    酿酒酵母SIR3重组蛋白
  • 货号：
    CSB-BP356918SVG
  • 规格：
  • 来源：
    Baculovirus
  • 其他：
  • 中文名称：
    酿酒酵母SIR3重组蛋白
  • 货号：
    CSB-MP356918SVG
  • 规格：
  • 来源：
    Mammalian cell
  • 其他：

产品详情

  • 纯度：
    >85% (SDS-PAGE)
  • 基因名：
    SIR3
  • Uniprot No.：
    P06701
  • 别名：
    SIR3; CMT1; MAR2; STE8; YLR442C; L9753.10Regulatory protein SIR3; Silent information regulator 3
  • 种属：
    Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
  • 蛋白长度：
    Partial
  • 蛋白标签：
    Tag type will be determined during the manufacturing process.
    The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
  • 产品提供形式：
    Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 复溶：
    We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
  • 储存条件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保质期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 货期：
    Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
    Note: All of our proteins are default shipped with normal blue ice packs, if you request to ship with dry ice, please communicate with us in advance and extra fees will be charged.
  • 注意事项：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet ：
    Please contact us to get it.

产品评价

靶点详情

  • 功能：
    The proteins SIR1 through SIR4 are required for transcriptional repression of the silent mating type loci, HML and HMR. The proteins SIR2 through SIR4 repress mulitple loci by modulating chromatin structure. Involves the compaction of chromatin fiber into a more condensed form.
  • 基因功能参考文献：
    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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  • 亚细胞定位：
    Nucleus.
  • 数据库链接：

    KEGG: sce:YLR442C

    STRING: 4932.YLR442C

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