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

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.
Mesh Terms:
Acetylation, Binding Sites, Chromatin Immunoprecipitation, Cluster Analysis, Gene Expression Profiling, Genome, Fungal, Histone Acetyltransferases, Histones, Lysine, Molecular Chaperones, Mutation, Nucleosomes, Oligonucleotide Array Sequence Analysis, Protein Binding, RNA Polymerase II, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Transcription, Genetic
Mol. Cell. Biol.
Date: Aug. 01, 2009
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