Vps75, a new yeast member of the NAP histone chaperone
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Vps75, a new yeast member of the NAP histone chaperone. / Selth, Luke; Svejstrup, Jesper Q.
In: Journal of Biological Chemistry, Vol. 282, No. 17, 27.04.2007, p. 12358-12362.Research output: Contribution to journal › Journal article › Research › peer-review
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TY - JOUR
T1 - Vps75, a new yeast member of the NAP histone chaperone
AU - Selth, Luke
AU - Svejstrup, Jesper Q.
PY - 2007/4/27
Y1 - 2007/4/27
N2 - 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 vps75Δ cells are insensitive to hydroxyurea, suggesting that although Rtt109 and Vps75 associate and are likely to be functionally connected, they also have separate roles.
AB - 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 vps75Δ cells are insensitive to hydroxyurea, suggesting that although Rtt109 and Vps75 associate and are likely to be functionally connected, they also have separate roles.
U2 - 10.1074/jbc.C700012200
DO - 10.1074/jbc.C700012200
M3 - Journal article
C2 - 17344218
AN - SCOPUS:34250309212
VL - 282
SP - 12358
EP - 12362
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 17
ER -
ID: 331022537