VPS75 cDNA ORF clone, Saccharomyces cerevisiae S288C

The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its evolutionary implications.
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Life with 6000 genes.
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Science (New York, N.Y.)274(5287)546, 563-7(1996 Oct)

he model provides a molecular basis for the involvement of both Vps75 and Asf1 in Rtt109 catalysed histone H3 K9 acetylation. In the absence of Asf1 this model can be used to generate a complex consisting of a reconfigured Vps75 tetramer bound to a H3-H4 tetramer.
Title: The histone chaperone Vps75 forms multiple oligomeric assemblies capable of mediating exchange between histone H3-H4 tetramers and Asf1-H3-H4 complexes.

Vps75 and Asf1 both enhance Rtt109 acetylation for H3/H4
Title: Utilizing targeted mass spectrometry to demonstrate Asf1-dependent increases in residue specificity for Rtt109-Vps75 mediated histone acetylation.

Rtt109-Vps75 preferentially acetylates H3 K9 and K23
Title: Chaperone-mediated acetylation of histones by Rtt109 identified by quantitative proteomics.

findings show that Nap1 and Vps75 regulate cryptic transcription observed in the absence of Ctk1. Rtt109 acetylation of H3 K9 also plays a role in this pathway, and both Vps75 and Nap1 promote acetylation of H3 in the ORF.
Title: Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation.

Data show that Rtt109 nuclear localization depends on Vps75, and nuclear localization of the Vps75-Rtt109 complex is not critical for Rtt109-dependent functions.
Title: Interaction with the histone chaperone Vps75 promotes nuclear localization and HAT activity of Rtt109 in vivo.