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

Harvard

Selth, L & Svejstrup, JQ 2007, 'Vps75, a new yeast member of the NAP histone chaperone', Journal of Biological Chemistry, vol. 282, no. 17, pp. 12358-12362. https://doi.org/10.1074/jbc.C700012200

APA

Selth, L., & Svejstrup, J. Q. (2007). Vps75, a new yeast member of the NAP histone chaperone. Journal of Biological Chemistry, 282(17), 12358-12362. https://doi.org/10.1074/jbc.C700012200

Vancouver

Selth L, Svejstrup JQ. Vps75, a new yeast member of the NAP histone chaperone. Journal of Biological Chemistry. 2007 Apr 27;282(17):12358-12362. https://doi.org/10.1074/jbc.C700012200

Author

Selth, Luke ; Svejstrup, Jesper Q. / Vps75, a new yeast member of the NAP histone chaperone. In: Journal of Biological Chemistry. 2007 ; Vol. 282, No. 17. pp. 12358-12362.

Bibtex

@article{a9d48679fa434085848ac491e405a613,
title = "Vps75, a new yeast member of the NAP histone chaperone",
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 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.",
author = "Luke Selth and Svejstrup, {Jesper Q.}",
year = "2007",
month = apr,
day = "27",
doi = "10.1074/jbc.C700012200",
language = "English",
volume = "282",
pages = "12358--12362",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "17",

}

RIS

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