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An rtt109-independent role for vps75 in transcription-associated nucleosome dynamics.

Authors
  • Selth, Luke A
  • Lorch, Yahli
  • Ocampo-Hafalla, Maria T
  • Mitter, Richard
  • Shales, Michael
  • Krogan, Nevan J
  • Kornberg, Roger D
  • Svejstrup, Jesper Q
Type
Published Article
Journal
Molecular and Cellular Biology
Publisher
American Society for Microbiology
Publication Date
Aug 01, 2009
Volume
29
Issue
15
Pages
4220–4234
Identifiers
DOI: 10.1128/MCB.01882-08
PMID: 19470761
Source
Medline
License
Unknown

Abstract

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. Analysis of epistatic miniarray profiles showed that VPS75 genetically interacts with factors involved in transcription regulation whereas RTT109 clusters with genes linked to DNA replication/repair. Additional genetic and biochemical experiments revealed a close relationship between Vps75 and RNA polymerase II. Furthermore, Vps75 is recruited to activated genes in an Rtt109-independent manner, and its genome-wide association with genes correlates with transcription rate. Expression microarray analysis identified a number of genes whose normal expression depends on VPS75. Interestingly, histone H2B dynamics at some of these genes are consistent with a role for Vps75 in histone H2A/H2B eviction/deposition during transcription. Indeed, reconstitution of nucleosome disassembly using the ATP-dependent chromatin remodeler Rsc and Vps75 revealed that these proteins can cooperate to remove H2A/H2B dimers from nucleosomes. These results indicate a role for Vps75 in nucleosome dynamics during transcription, and importantly, this function appears to be largely independent of Rtt109.

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