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.