RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes

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RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes. / Sebastiaan Winkler, G.; Petrakis, Thodoris G.; Ethelberg, Steen; Tokunaga, Masao; Erdjument-Bromage, Hediye; Tempst, Paul; Svejstrup, Jesper Q.

In: Journal of Biological Chemistry, Vol. 276, No. 35, 31.08.2001, p. 32743-32749.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Sebastiaan Winkler, G, Petrakis, TG, Ethelberg, S, Tokunaga, M, Erdjument-Bromage, H, Tempst, P & Svejstrup, JQ 2001, 'RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes', Journal of Biological Chemistry, vol. 276, no. 35, pp. 32743-32749. https://doi.org/10.1074/jbc.M105303200

APA

Sebastiaan Winkler, G., Petrakis, T. G., Ethelberg, S., Tokunaga, M., Erdjument-Bromage, H., Tempst, P., & Svejstrup, J. Q. (2001). RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes. Journal of Biological Chemistry, 276(35), 32743-32749. https://doi.org/10.1074/jbc.M105303200

Vancouver

Sebastiaan Winkler G, Petrakis TG, Ethelberg S, Tokunaga M, Erdjument-Bromage H, Tempst P et al. RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes. Journal of Biological Chemistry. 2001 Aug 31;276(35):32743-32749. https://doi.org/10.1074/jbc.M105303200

Author

Sebastiaan Winkler, G. ; Petrakis, Thodoris G. ; Ethelberg, Steen ; Tokunaga, Masao ; Erdjument-Bromage, Hediye ; Tempst, Paul ; Svejstrup, Jesper Q. / RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes. In: Journal of Biological Chemistry. 2001 ; Vol. 276, No. 35. pp. 32743-32749.

Bibtex

@article{391c1ac577cf42b7a63fe35aec247152,
title = "RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes",
abstract = "Elongator is a histone acetyltransferase complex that associates with the elongating form of RNA polymerase II. We purified Elongator to virtual homogeneity via a rapid three-step procedure based largely on affinity chromatography. The purified factor, holo-Elongator, is a labile six-subunit factor composed of two discrete subcomplexes: one comprised of the previously identified Elp1, Elp2, and Elp3 proteins and another comprised of three novel polypeptides, termed Elp4, Elp5, and Elp6. Disruption of the yeast genes encoding the new Elongator proteins confers phenotypes indistinguishable from those previously described for the other elp mutants, and concomitant disruption of genes encoding proteins in either subcomplex does not confer new phenotypes. Taken together, our results indicate that holo-Elongator is a functional entity in vitro as well as in vivo. Metazoan homologues of Elp1 and Elp3 have previously been reported. We cloned the human homologue of yeast ELP4 and show that this gene is ubiquitously expressed in human tissues.",
author = "{Sebastiaan Winkler}, G. and Petrakis, {Thodoris G.} and Steen Ethelberg and Masao Tokunaga and Hediye Erdjument-Bromage and Paul Tempst and Svejstrup, {Jesper Q.}",
year = "2001",
month = aug,
day = "31",
doi = "10.1074/jbc.M105303200",
language = "English",
volume = "276",
pages = "32743--32749",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "35",

}

RIS

TY - JOUR

T1 - RNA Polymerase II Elongator Holoenzyme Is Composed of Two Discrete Subcomplexes

AU - Sebastiaan Winkler, G.

AU - Petrakis, Thodoris G.

AU - Ethelberg, Steen

AU - Tokunaga, Masao

AU - Erdjument-Bromage, Hediye

AU - Tempst, Paul

AU - Svejstrup, Jesper Q.

PY - 2001/8/31

Y1 - 2001/8/31

N2 - Elongator is a histone acetyltransferase complex that associates with the elongating form of RNA polymerase II. We purified Elongator to virtual homogeneity via a rapid three-step procedure based largely on affinity chromatography. The purified factor, holo-Elongator, is a labile six-subunit factor composed of two discrete subcomplexes: one comprised of the previously identified Elp1, Elp2, and Elp3 proteins and another comprised of three novel polypeptides, termed Elp4, Elp5, and Elp6. Disruption of the yeast genes encoding the new Elongator proteins confers phenotypes indistinguishable from those previously described for the other elp mutants, and concomitant disruption of genes encoding proteins in either subcomplex does not confer new phenotypes. Taken together, our results indicate that holo-Elongator is a functional entity in vitro as well as in vivo. Metazoan homologues of Elp1 and Elp3 have previously been reported. We cloned the human homologue of yeast ELP4 and show that this gene is ubiquitously expressed in human tissues.

AB - Elongator is a histone acetyltransferase complex that associates with the elongating form of RNA polymerase II. We purified Elongator to virtual homogeneity via a rapid three-step procedure based largely on affinity chromatography. The purified factor, holo-Elongator, is a labile six-subunit factor composed of two discrete subcomplexes: one comprised of the previously identified Elp1, Elp2, and Elp3 proteins and another comprised of three novel polypeptides, termed Elp4, Elp5, and Elp6. Disruption of the yeast genes encoding the new Elongator proteins confers phenotypes indistinguishable from those previously described for the other elp mutants, and concomitant disruption of genes encoding proteins in either subcomplex does not confer new phenotypes. Taken together, our results indicate that holo-Elongator is a functional entity in vitro as well as in vivo. Metazoan homologues of Elp1 and Elp3 have previously been reported. We cloned the human homologue of yeast ELP4 and show that this gene is ubiquitously expressed in human tissues.

U2 - 10.1074/jbc.M105303200

DO - 10.1074/jbc.M105303200

M3 - Journal article

C2 - 11435442

AN - SCOPUS:0035980015

VL - 276

SP - 32743

EP - 32749

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 35

ER -

ID: 331575710