Reference: Selth L and Svejstrup JQ (2007) Vps75, A New Yeast Member of the NAP Histone Chaperone Family. J Biol Chem 282(17):12358-62

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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 binds histones with a strong preference for 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 K56). Cells lacking RTT109 are sensitive to hydroxyurea, pointing to a role in replication. We show that VPS75 is not required for H3 K56 acetylation and that vps75 cells are insensitive to hydroxyurea, suggesting that although Rtt109 and Vps75 associate and are likely to be functionally connected, they also have separate roles.

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Journal Article
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Selth L, Svejstrup JQ
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