Abstract
Homologues of nucleosome assembly protein 1 (NAP1) are found throughout eukaryotes. Here we identify and characterize a new NAP family histone chaperone from budding yeast, named Vps75. Purified Vps75 preferentially binds histone H3/H4 tetramers and is capable of assembling nucleosomes in vitro. In vivo, Vps75 is associated with the chromatin of both active and inactive genes and telomeres. Others have previously reported that Vps75 forms a complex with Rtt109, required for acetylation of histone H3 lysine 56 (H3 Lys-56). Cells lacking RTT109 are sensitive to hydroxyurea, pointing to a role in replication. We show that VPS75 is not required for H3 Lys-56 acetylation and that vps75Delta cells are insensitive to hydroxyurea, suggesting that although Rtt109 and Vps75 associate and are likely to be functionally connected, they also have separate roles.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Chromatin Assembly and Disassembly / drug effects
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Chromatin Assembly and Disassembly / physiology
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DNA Replication / drug effects
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DNA Replication / physiology*
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Drug Resistance, Fungal / genetics
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Histones / genetics
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Histones / metabolism*
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Hydroxyurea / pharmacology
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Molecular Chaperones / genetics
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Molecular Chaperones / metabolism*
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Nucleic Acid Synthesis Inhibitors / pharmacology
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Nucleosomes / genetics
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Nucleosomes / metabolism
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae / metabolism*
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Saccharomyces cerevisiae Proteins / genetics
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Saccharomyces cerevisiae Proteins / metabolism
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Telomere / genetics
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Telomere / metabolism
Substances
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Histones
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Molecular Chaperones
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Nucleic Acid Synthesis Inhibitors
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Nucleosomes
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Rtt106 protein, S cerevisiae
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Saccharomyces cerevisiae Proteins
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Hydroxyurea