Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo

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Standard

Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. / Winkler, G. Sebastiaan; Kristjuhan, Arnold; Erdjument-Bromage, Hediye; Tempst, Paul; Svejstrup, Jesper Q.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 99, Nr. 6, 19.03.2002, s. 3517-3522.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Winkler, GS, Kristjuhan, A, Erdjument-Bromage, H, Tempst, P & Svejstrup, JQ 2002, 'Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo', Proceedings of the National Academy of Sciences of the United States of America, bind 99, nr. 6, s. 3517-3522. https://doi.org/10.1073/pnas.022042899

APA

Winkler, G. S., Kristjuhan, A., Erdjument-Bromage, H., Tempst, P., & Svejstrup, J. Q. (2002). Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. Proceedings of the National Academy of Sciences of the United States of America, 99(6), 3517-3522. https://doi.org/10.1073/pnas.022042899

Vancouver

Winkler GS, Kristjuhan A, Erdjument-Bromage H, Tempst P, Svejstrup JQ. Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. Proceedings of the National Academy of Sciences of the United States of America. 2002 mar. 19;99(6):3517-3522. https://doi.org/10.1073/pnas.022042899

Author

Winkler, G. Sebastiaan ; Kristjuhan, Arnold ; Erdjument-Bromage, Hediye ; Tempst, Paul ; Svejstrup, Jesper Q. / Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo. I: Proceedings of the National Academy of Sciences of the United States of America. 2002 ; Bind 99, Nr. 6. s. 3517-3522.

Bibtex

@article{e5c469ded5824da38cd64abb76f1d6e6,
title = "Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo",
abstract = "The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. Here we show that, in contrast to the isolated Elp3 subunit, the activity of intact Elongator complex is directed specifically toward the amino-terminal tails of histone H3 and H4, and that Elongator can acetylate both core histones and nucleosomal substrates. The predominant acetylation sites are lysine-14 of histone H3 and lysine-8 of histone H4. The three smallest Elongator subunits-Elp4, Elp5, and Elp6-are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. By using chromatin immunoprecipitation, we show that the levels of multiply acetylated histone H3 and H4 in chromatin are decreased in vivo in yeast cells lacking ELP3.",
author = "Winkler, {G. Sebastiaan} and Arnold Kristjuhan and Hediye Erdjument-Bromage and Paul Tempst and Svejstrup, {Jesper Q.}",
year = "2002",
month = mar,
day = "19",
doi = "10.1073/pnas.022042899",
language = "English",
volume = "99",
pages = "3517--3522",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "6",

}

RIS

TY - JOUR

T1 - Elongator is a histone H3 and H4 acetyltransferase important for normal histone acetylation levels in vivo

AU - Winkler, G. Sebastiaan

AU - Kristjuhan, Arnold

AU - Erdjument-Bromage, Hediye

AU - Tempst, Paul

AU - Svejstrup, Jesper Q.

PY - 2002/3/19

Y1 - 2002/3/19

N2 - The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. Here we show that, in contrast to the isolated Elp3 subunit, the activity of intact Elongator complex is directed specifically toward the amino-terminal tails of histone H3 and H4, and that Elongator can acetylate both core histones and nucleosomal substrates. The predominant acetylation sites are lysine-14 of histone H3 and lysine-8 of histone H4. The three smallest Elongator subunits-Elp4, Elp5, and Elp6-are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. By using chromatin immunoprecipitation, we show that the levels of multiply acetylated histone H3 and H4 in chromatin are decreased in vivo in yeast cells lacking ELP3.

AB - The elongating, hyperphosphorylated form of RNA polymerase II is associated with the Elongator complex, which has the histone acetyltransferase (HAT) Elp3 as a subunit. Here we show that, in contrast to the isolated Elp3 subunit, the activity of intact Elongator complex is directed specifically toward the amino-terminal tails of histone H3 and H4, and that Elongator can acetylate both core histones and nucleosomal substrates. The predominant acetylation sites are lysine-14 of histone H3 and lysine-8 of histone H4. The three smallest Elongator subunits-Elp4, Elp5, and Elp6-are required for HAT activity, and Elongator binds to both naked and nucleosomal DNA. By using chromatin immunoprecipitation, we show that the levels of multiply acetylated histone H3 and H4 in chromatin are decreased in vivo in yeast cells lacking ELP3.

U2 - 10.1073/pnas.022042899

DO - 10.1073/pnas.022042899

M3 - Journal article

C2 - 11904415

AN - SCOPUS:0037133562

VL - 99

SP - 3517

EP - 3522

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 6

ER -

ID: 331042066