Vps75, A New Yeast Member of the NAP Histone Chaperone Family

Luke Selth, Jesper Q. Svejstrup

Research output: Contribution to journalArticle

54 Citations (Scopus)

Abstract

Homologues of nucleosome assembly protein 1 (NAP1) are found throughout eukaryotes. 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. In vivo, Vps75 is associated with the chromatin of both active and inactive genes and telomeres. Others have previously reported that Vps75 forms a complex with Rtt109, required for acetylation of histone H3 lysine 56 (H3 Lys-56). Cells lacking RTT109 are sensitive to hydroxyurea, pointing to a role in replication. We show that VPS75 is not required for H3 Lys-56 acetylation and that vps75Δ cells are insensitive to hydroxyurea, suggesting that although Rtt109 and Vps75 associate and are likely to be functionally connected, they also have separate roles.

Original languageEnglish
Pages (from-to)12358-12362
Number of pages5
JournalJournal of Biological Chemistry
Volume282
Issue number17
DOIs
Publication statusPublished - 27 Apr 2007
Externally publishedYes

Fingerprint Dive into the research topics of 'Vps75, A New Yeast Member of the NAP Histone Chaperone Family'. Together they form a unique fingerprint.

  • Cite this