VPS75

Summary

Gene Symbol: VPS75
Description: Vps75p
Alias: Vps75p
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Selth L, Lorch Y, Ocampo Hafalla M, Mitter R, Shales M, Krogan N, et al. An rtt109-independent role for vps75 in transcription-associated nucleosome dynamics. Mol Cell Biol. 2009;29:4220-34 pubmed publisher
    The histone chaperone Vps75 forms a complex with, and stimulates the activity of, the histone acetyltransferase Rtt109. However, Vps75 can also be isolated on its own and might therefore possess Rtt109-independent functions...
  2. Selth L, Svejstrup J. Vps75, a new yeast member of the NAP histone chaperone family. J Biol Chem. 2007;282:12358-62 pubmed
    ..Here we identify and characterize a new NAP family histone chaperone from budding yeast, named Vps75. Purified Vps75 preferentially binds histone H3/H4 tetramers and is capable of assembling nucleosomes in vitro...
  3. Keck K, Pemberton L. Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo. Traffic. 2011;12:826-39 pubmed publisher
    ..Rtt109 associates with and is stabilized by Nap1 family histone chaperone Vps75. Our data suggest Vps75 and Nap1 have some overlapping functions despite their different cellular localization and ..
  4. Su D, Hu Q, Zhou H, Thompson J, Xu R, Zhang Z, et al. Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex. J Biol Chem. 2011;286:15625-9 pubmed publisher
    The histone chaperone Vps75 presents the remarkable property of stimulating the Rtt109-dependent acetylation of several histone H3 lysine residues within (H3-H4)(2) tetramers...
  5. Albaugh B, Kolonko E, Denu J. Kinetic mechanism of the Rtt109-Vps75 histone acetyltransferase-chaperone complex. Biochemistry. 2010;49:6375-85 pubmed publisher
    ..Rtt109 associates with the NAP1 family histone chaperone Vps75 and stimulates histone acetylation...
  6. Park Y, Sudhoff K, Andrews A, Stargell L, Luger K. Histone chaperone specificity in Rtt109 activation. Nat Struct Mol Biol. 2008;15:957-64 pubmed
    ..Rtt109 forms a complex with the chaperone Vps75 in vivo and is implicated in DNA replication and repair...
  7. Berndsen C, Tsubota T, Lindner S, Lee S, Holton J, Kaufman P, et al. Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nat Struct Mol Biol. 2008;15:948-56 pubmed
    ..In vitro analysis of Rtt109 revealed that Vps75, a Nap1 family histone chaperone, could also stimulate Rtt109-dependent acetylation of H3K56...
  8. Tang Y, Holbert M, Wurtele H, Meeth K, Rocha W, Gharib M, et al. Fungal Rtt109 histone acetyltransferase is an unexpected structural homolog of metazoan p300/CBP. Nat Struct Mol Biol. 2008;15:738-45 pubmed publisher
    ..conservation with other known HATs and depends on association with either of two histone chaperones, Asf1 or Vps75, for HAT activity...
  9. Abshiru N, Ippersiel K, Tang Y, Yuan H, Marmorstein R, Verreault A, et al. Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics. J Proteomics. 2013;81:80-90 pubmed publisher
    Rtt109 is a fungal-specific histone acetyltransferase (HAT) that associates with either Vps75 or Asf1 to acetylate histone H3...

More Information

Publications21

  1. Xue Y, Kowalska A, Grabowska K, Przybyt K, Cichewicz M, Del Rosario B, et al. Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation. Mol Cell Biol. 2013;33:1645-56 pubmed publisher
    ..The Saccharomyces cerevisiae proteins Nap1 and Vps75 are structurally related, evolutionarily conserved histone chaperones...
  2. Radovani E, Cadorin M, Shams T, El Rass S, Karsou A, Kim H, et al. The carboxyl terminus of Rtt109 functions in chaperone control of histone acetylation. Eukaryot Cell. 2013;12:654-64 pubmed publisher
    ..Rtt109-mediated H3 acetylation involves two histone chaperones, Asf1 and Vps75. In vivo, Rtt109 requires both chaperones for histone H3 lysine 9 acetylation (H3K9ac) but only Asf1 for full ..
  3. Kolonko E, Albaugh B, Lindner S, Chen Y, Satyshur K, Arnold K, et al. Catalytic activation of histone acetyltransferase Rtt109 by a histone chaperone. Proc Natl Acad Sci U S A. 2010;107:20275-80 pubmed publisher
    ..of a HAT whose specificity and catalytic activity require association with either of two histone chaperones, Vps75 or Asf1...
  4. Tang Y, Meeth K, Jiang E, Luo C, Marmorstein R. Structure of Vps75 and implications for histone chaperone function. Proc Natl Acad Sci U S A. 2008;105:12206-11 pubmed publisher
    The vacuolar protein sorting 75 (Vps75) histone chaperone participates in chromatin assembly and disassembly at both active and inactive genes through the preferential binding to histone H3-H4...
  5. Tang Y, Holbert M, Delgoshaie N, Wurtele H, Guillemette B, Meeth K, et al. Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation. Structure. 2011;19:221-31 pubmed publisher
    ..by acetylating K9, K27, and K56 of histone H3 through interaction with either of two distinct histone chaperones, Vps75 or Asf1...
  6. Bowman A, Hammond C, Stirling A, Ward R, Shang W, El Mkami H, et al. The histone chaperones Vps75 and Nap1 form ring-like, tetrameric structures in solution. Nucleic Acids Res. 2014;42:6038-51 pubmed publisher
    ..The two NAP-1 fold histone chaperones in budding yeast, Vps75 and Nap1, have previously been crystalized in a characteristic homodimeric conformation...
  7. Wang A, Aristizabal M, Ryan C, Krogan N, Kobor M. Key functional regions in the histone variant H2A.Z C-terminal docking domain. Mol Cell Biol. 2011;31:3871-84 pubmed publisher
    ..Z deposition complex SWR1-C, the histone chaperone Chz1, and histone H2B. These data are consistent with a model in which retaining the variant in chromatin after its deposition by SWR1-C is a crucial determinant of its function. ..
  8. Hammond C, Sundaramoorthy R, Larance M, Lamond A, Stevens M, El Mkami H, et al. The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes. Nucleic Acids Res. 2016;44:6157-72 pubmed publisher
    b>Vps75 is a histone chaperone that has been historically characterized as homodimer by X-ray crystallography. In this study, we present a crystal structure containing two related tetrameric forms of Vps75 within the crystal lattice...
  9. Lopes da Rosa J, Bajaj V, Spoonamore J, Kaufman P. A small molecule inhibitor of fungal histone acetyltransferase Rtt109. Bioorg Med Chem Lett. 2013;23:2853-9 pubmed publisher
    ..This compound inhibits Rtt109 regardless of which histone chaperone cofactor protein (Asf1 or Vps75) is present, and appears to inhibit Rtt109 via a tight-binding, uncompetitive mechanism.
  10. Jessulat M, Alamgir M, Salsali H, Greenblatt J, Xu J, Golshani A. Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch Biochem Biophys. 2008;469:157-64 pubmed
    ..Tandem-affinity purification of Rtt109 recovered Vps75 as a physical interacting protein...
  11. Burgess R, Zhou H, Han J, Zhang Z. A role for Gcn5 in replication-coupled nucleosome assembly. Mol Cell. 2010;37:469-80 pubmed publisher
    ..These results demonstrate that Gcn5 regulates RC nucleosome assembly, in part, by promoting H3 association with CAF-1 via H3 acetylation. ..
  12. Kuo Y, Henry R, Huang L, Chen X, Stargell L, Andrews A. Utilizing targeted mass spectrometry to demonstrate Asf1-dependent increases in residue specificity for Rtt109-Vps75 mediated histone acetylation. PLoS ONE. 2015;10:e0118516 pubmed publisher
    In Saccharomyces cerevisiae, Rtt109, a lysine acetyltransferase (KAT), associates with a histone chaperone, either Vps75 or Asf1...