VPS75 Vps75p [Saccharomyces cerevisiae S288C] - Gene

Summary

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Official Symbol: VPS75
Official Full Name: Vps75p
Primary source: SGD:S000005190
Locus tag: YNL246W
See related: AllianceGenome:SGD:S000005190; FungiDB:YNL246W; VEuPathDB:YNL246W
Gene type: protein coding
RefSeq status: REVIEWED
Organism: Saccharomyces cerevisiae S288C (strain: S288C)
Lineage: Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Summary: Enables acetyltransferase activator activity and histone binding activity. Involved in double-strand break repair via nonhomologous end joining; nucleosome assembly; and positive regulation of histone acetylation. Located in cytosol and nucleus. Colocalizes with chromatin. Human ortholog(s) of this gene implicated in autosomal dominant non-syndromic intellectual disability; gonadal dysgenesis; and sudden infant death syndrome. Orthologous to several human genes including SET (SET nuclear proto-oncogene); TSPY10 (testis specific protein Y-linked 10); and TSPY2 (testis specific protein Y-linked 2). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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See VPS75 in Genome Data Viewer

Location:: chromosome: XIV

Exon count:: 2

Sequence:: Chromosome: XIV; NC_001146.8 (185460..186349)

Chromosome XIV - NC_001146.8 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:: NC_001146.8

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4.
Title: Stoichiometry of Rtt109 complexes with Vps75 and histones H3-H4.
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.
Histone chaperones, Vps75 or Asf1, dictate Histone acetyltransferase, Rtt109, substrate specificity through distinct mechanisms.
Title: Structure of the Rtt109-AcCoA/Vps75 complex and implications for chaperone-mediated histone acetylation.
the basis for the enhanced acetylation of histone H3 tail residues by Vps75-Rtt109.
Title: Structure and histone binding properties of the Vps75-Rtt109 chaperone-lysine acetyltransferase complex.
Results indicate a role for Vps75 in nucleosome dynamics during transcription, and importantly, this function appears to be largely independent of Rtt109.
Title: An rtt109-independent role for vps75 in transcription-associated nucleosome dynamics.
probed the molecular functions of Vps75 and the Rtt109-Vps75 complex through biochemical, structural and genetic means
Title: Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75.

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Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Homology

Orthologs from OrthoDB

Gene Ontology Provided by SGD

Function	Evidence Code	Pubs
enables acetyltransferase activator activity	IDA Inferred from Direct Assay more info	PubMed
enables acetyltransferase activator activity	IMP Inferred from Mutant Phenotype more info	PubMed
enables chromatin binding	IBA Inferred from Biological aspect of Ancestor more info
enables histone binding	IBA Inferred from Biological aspect of Ancestor more info
enables histone binding	IDA Inferred from Direct Assay more info	PubMed
enables histone binding	IPI Inferred from Physical Interaction more info	PubMed

Process	Evidence Code	Pubs
involved_in double-strand break repair via nonhomologous end joining	IMP Inferred from Mutant Phenotype more info	PubMed
involved_in double-strand break repair via nonhomologous end joining	IPI Inferred from Physical Interaction more info	PubMed
involved_in nucleosome assembly	IDA Inferred from Direct Assay more info	PubMed
involved_in nucleosome assembly	IEA Inferred from Electronic Annotation more info
involved_in protein transport	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
located_in chromatin	IBA Inferred from Biological aspect of Ancestor more info
located_in chromatin	IDA Inferred from Direct Assay more info	PubMed
located_in cytosol	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	HDA more info	PubMed
is_active_in nucleus	IBA Inferred from Biological aspect of Ancestor more info
located_in nucleus	IDA Inferred from Direct Assay more info	PubMed
located_in nucleus	IEA Inferred from Electronic Annotation more info

General protein information

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Preferred Names: Vps75p

NP_014153.1

NAP family histone chaperone; binds to histones and Rtt109p, stimulating histone acetyltransferase activity; possesses nucleosome assembly activity in vitro; proposed role in vacuolar protein sorting and in double-strand break repair; protein abundance increases in response to DNA replication stress; relocalizes to the cytosol in response to hypoxia