A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme

Research output: Contribution to journal › Journal article › Research › peer-review

Standard

A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. / Wittschieben, Birgitte; Otero, Gabriel; De Bizemont, Therese; Fellows, Jane; Erdjument-Bromage, Hediye; Ohba, Reiko; Li, Yang; Allis, C. David; Tempst, Paul; Svejstrup, Jesper Q.

In: Molecular Cell, Vol. 4, No. 1, 07.1999, p. 123-128.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Wittschieben, B, Otero, G, De Bizemont, T, Fellows, J, Erdjument-Bromage, H, Ohba, R, Li, Y, Allis, CD, Tempst, P & Svejstrup, JQ 1999, 'A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme', Molecular Cell, vol. 4, no. 1, pp. 123-128. https://doi.org/10.1016/S1097-2765(00)80194-X

APA

Wittschieben, B., Otero, G., De Bizemont, T., Fellows, J., Erdjument-Bromage, H., Ohba, R., Li, Y., Allis, C. D., Tempst, P., & Svejstrup, J. Q. (1999). A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. Molecular Cell, 4(1), 123-128. https://doi.org/10.1016/S1097-2765(00)80194-X

Vancouver

Wittschieben B, Otero G, De Bizemont T, Fellows J, Erdjument-Bromage H, Ohba R et al. A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. Molecular Cell. 1999 Jul;4(1):123-128. https://doi.org/10.1016/S1097-2765(00)80194-X

Author

Wittschieben, Birgitte ; Otero, Gabriel ; De Bizemont, Therese ; Fellows, Jane ; Erdjument-Bromage, Hediye ; Ohba, Reiko ; Li, Yang ; Allis, C. David ; Tempst, Paul ; Svejstrup, Jesper Q. / A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme. In: Molecular Cell. 1999 ; Vol. 4, No. 1. pp. 123-128.

Bibtex

@article{ee689cbdcee54ad3a1658b0ada3e0416,
title = "A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme",
abstract = "The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a rote for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.",
author = "Birgitte Wittschieben and Gabriel Otero and {De Bizemont}, Therese and Jane Fellows and Hediye Erdjument-Bromage and Reiko Ohba and Yang Li and Allis, {C. David} and Paul Tempst and Svejstrup, {Jesper Q.}",
note = "Funding Information: The project was supported by grants from the Imperial Cancer Research Fund and the Human Frontier Science Project (RG0193/97) to J. Q. S., by EU fellowships to B. {\O}. W. and T. d. B., by a Bank of America–Giannini Foundation Medical Research Fellowship to Y. L., by an NIH grant (GM53512) to C. D. A., and by an NCI core grant (P30 CA08748) to P. T. B. {\O}. W. has published previously under the name B. {\O}. Petersen. We are indebted to ICRF service facilities, especially cell culture and fermentation services, for their help. A large number of colleagues, especially Alain Verrault, Rick Wood, and Brad Cairns, are thanked for their comments on the manuscript.",
year = "1999",
month = jul,
doi = "10.1016/S1097-2765(00)80194-X",
language = "English",
volume = "4",
pages = "123--128",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - A novel histone acetyltransferase is an integral subunit of elongating RNA polymerase II holoenzyme

AU - Wittschieben, Birgitte

AU - Otero, Gabriel

AU - De Bizemont, Therese

AU - Fellows, Jane

AU - Erdjument-Bromage, Hediye

AU - Ohba, Reiko

AU - Li, Yang

AU - Allis, C. David

AU - Tempst, Paul

AU - Svejstrup, Jesper Q.

N1 - Funding Information: The project was supported by grants from the Imperial Cancer Research Fund and the Human Frontier Science Project (RG0193/97) to J. Q. S., by EU fellowships to B. Ø. W. and T. d. B., by a Bank of America–Giannini Foundation Medical Research Fellowship to Y. L., by an NIH grant (GM53512) to C. D. A., and by an NCI core grant (P30 CA08748) to P. T. B. Ø. W. has published previously under the name B. Ø. Petersen. We are indebted to ICRF service facilities, especially cell culture and fermentation services, for their help. A large number of colleagues, especially Alain Verrault, Rick Wood, and Brad Cairns, are thanked for their comments on the manuscript.

PY - 1999/7

Y1 - 1999/7

N2 - The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a rote for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.

AB - The elongator complex is a major component of the RNA polymerase II (RNAPII) holoenzyme responsible for transcriptional elongation in yeast. Here we identify Elp3, the 60-kilodalton subunit of elongator/RNAPII holoenzyme, as a highly conserved histone acetyltransferase (HAT) capable of acetylating core histones in vitro. In vivo, ELP3 gene deletion confers typical elp phenotypes such as slow growth adaptation, slow gene activation, and temperature sensitivity. These results suggest a rote for a novel, tightly RNAPII-associated HAT in transcription of DNA packaged in chromatin.

UR - http://www.scopus.com/inward/record.url?scp=0033166761&partnerID=8YFLogxK

U2 - 10.1016/S1097-2765(00)80194-X

DO - 10.1016/S1097-2765(00)80194-X

M3 - Journal article

C2 - 10445034

AN - SCOPUS:0033166761

VL - 4

SP - 123

EP - 128

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 1

ER -

ID: 331575433