Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation

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Standard

Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. / Otero, Gabriel; Fellows, Jane; Yang, Li; De Bizemont, Therese; Dirac, Annette M.G.; Gustafsson, Claes M.; Erdjument-Bromage, Hediye; Tempst, Paul; Svejstrup, Jesper Q.

I: Molecular Cell, Bind 3, Nr. 1, 01.1999, s. 109-118.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Otero, G, Fellows, J, Yang, L, De Bizemont, T, Dirac, AMG, Gustafsson, CM, Erdjument-Bromage, H, Tempst, P & Svejstrup, JQ 1999, 'Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation', Molecular Cell, bind 3, nr. 1, s. 109-118. https://doi.org/10.1016/S1097-2765(00)80179-3

APA

Otero, G., Fellows, J., Yang, L., De Bizemont, T., Dirac, A. M. G., Gustafsson, C. M., Erdjument-Bromage, H., Tempst, P., & Svejstrup, J. Q. (1999). Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Molecular Cell, 3(1), 109-118. https://doi.org/10.1016/S1097-2765(00)80179-3

Vancouver

Otero G, Fellows J, Yang L, De Bizemont T, Dirac AMG, Gustafsson CM o.a. Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. Molecular Cell. 1999 jan.;3(1):109-118. https://doi.org/10.1016/S1097-2765(00)80179-3

Author

Otero, Gabriel ; Fellows, Jane ; Yang, Li ; De Bizemont, Therese ; Dirac, Annette M.G. ; Gustafsson, Claes M. ; Erdjument-Bromage, Hediye ; Tempst, Paul ; Svejstrup, Jesper Q. / Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation. I: Molecular Cell. 1999 ; Bind 3, Nr. 1. s. 109-118.

Bibtex

@article{8db2eda5b99343a1a47becf47c582b61,
title = "Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation",
abstract = "The form of RNA polymerase II (RNAPII) engaged in transcriptional elongation was isolated. Elongating RNAPII was associated with a novel multisubunit complex, termed elongator, whose stable interaction was dependent on a hyperphosphorylated state of the RNAPII carboxy-terminal domain (CTD). A free form of elongator was also isolated, demonstrating the discrete nature of the complex, and free elongator could bind directly to RNAPII. The gene encoding the largest subunit of elongator, ELP1, was cloned. Phenotypes of yeast elp1Δ, cells demonstrated an involvement of elongator in transcriptional elongation as well as activation in vivo. Our data indicate that the transition from transcriptional initiation to elongation involves an exchange of the multiprotein mediator complex for elongator in a reaction coupled to CTD hyperphosphorylation.",
author = "Gabriel Otero and Jane Fellows and Li Yang and {De Bizemont}, Therese and Dirac, {Annette M.G.} and Gustafsson, {Claes M.} and Hediye Erdjument-Bromage and Paul Tempst and Svejstrup, {Jesper Q.}",
note = "Funding Information: The project was supported by the Imperial Cancer Research Fund, the Human Frontier Science Project (RG-193/97), by an EC fellowship (BMH4-CT96-5021) to T. d. B., by a Bank of America-Giannini Foundation Medical Research Fellowship to Y. L., and by a NCI core grant (P30 CA08748). We are indebted to Lynne Lacomis, Mary Lui, and Anita Grewal for help with mass spectrometric analysis, to Matthias Mann (Odense University, Denmark) for the PeptideSearch program, and to Hans Ronne, Rick Young, Dick Burgess, and Roger Kornberg for reagents used in this study. Noel Lowndes, Grant Hartzog, and Brad Cairns are thanked for their help and advice on yeast genetics, and Peter Verrijzer, Rick Wood, Roger Kornberg, and members of the Svejstrup lab for comments on the manuscript. ",
year = "1999",
month = jan,
doi = "10.1016/S1097-2765(00)80179-3",
language = "English",
volume = "3",
pages = "109--118",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - Elongator, a multisubunit component of a novel RNA polymerase II holoenzyme for transcriptional elongation

AU - Otero, Gabriel

AU - Fellows, Jane

AU - Yang, Li

AU - De Bizemont, Therese

AU - Dirac, Annette M.G.

AU - Gustafsson, Claes M.

AU - Erdjument-Bromage, Hediye

AU - Tempst, Paul

AU - Svejstrup, Jesper Q.

N1 - Funding Information: The project was supported by the Imperial Cancer Research Fund, the Human Frontier Science Project (RG-193/97), by an EC fellowship (BMH4-CT96-5021) to T. d. B., by a Bank of America-Giannini Foundation Medical Research Fellowship to Y. L., and by a NCI core grant (P30 CA08748). We are indebted to Lynne Lacomis, Mary Lui, and Anita Grewal for help with mass spectrometric analysis, to Matthias Mann (Odense University, Denmark) for the PeptideSearch program, and to Hans Ronne, Rick Young, Dick Burgess, and Roger Kornberg for reagents used in this study. Noel Lowndes, Grant Hartzog, and Brad Cairns are thanked for their help and advice on yeast genetics, and Peter Verrijzer, Rick Wood, Roger Kornberg, and members of the Svejstrup lab for comments on the manuscript.

PY - 1999/1

Y1 - 1999/1

N2 - The form of RNA polymerase II (RNAPII) engaged in transcriptional elongation was isolated. Elongating RNAPII was associated with a novel multisubunit complex, termed elongator, whose stable interaction was dependent on a hyperphosphorylated state of the RNAPII carboxy-terminal domain (CTD). A free form of elongator was also isolated, demonstrating the discrete nature of the complex, and free elongator could bind directly to RNAPII. The gene encoding the largest subunit of elongator, ELP1, was cloned. Phenotypes of yeast elp1Δ, cells demonstrated an involvement of elongator in transcriptional elongation as well as activation in vivo. Our data indicate that the transition from transcriptional initiation to elongation involves an exchange of the multiprotein mediator complex for elongator in a reaction coupled to CTD hyperphosphorylation.

AB - The form of RNA polymerase II (RNAPII) engaged in transcriptional elongation was isolated. Elongating RNAPII was associated with a novel multisubunit complex, termed elongator, whose stable interaction was dependent on a hyperphosphorylated state of the RNAPII carboxy-terminal domain (CTD). A free form of elongator was also isolated, demonstrating the discrete nature of the complex, and free elongator could bind directly to RNAPII. The gene encoding the largest subunit of elongator, ELP1, was cloned. Phenotypes of yeast elp1Δ, cells demonstrated an involvement of elongator in transcriptional elongation as well as activation in vivo. Our data indicate that the transition from transcriptional initiation to elongation involves an exchange of the multiprotein mediator complex for elongator in a reaction coupled to CTD hyperphosphorylation.

UR - http://www.scopus.com/inward/record.url?scp=0032971711&partnerID=8YFLogxK

U2 - 10.1016/S1097-2765(00)80179-3

DO - 10.1016/S1097-2765(00)80179-3

M3 - Journal article

C2 - 10024884

AN - SCOPUS:0032971711

VL - 3

SP - 109

EP - 118

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 1

ER -

ID: 331574464