Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD

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Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD. / Somesh, Baggavalli P.; Sigurdsson, Stefan; Saeki, Hideaki; Erdjument-Bromage, Hediye; Tempst, Paul; Svejstrup, Jesper Q.

I: Cell, Bind 129, Nr. 1, 06.04.2007, s. 57-68.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Somesh, BP, Sigurdsson, S, Saeki, H, Erdjument-Bromage, H, Tempst, P & Svejstrup, JQ 2007, 'Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD', Cell, bind 129, nr. 1, s. 57-68. https://doi.org/10.1016/j.cell.2007.01.046

APA

Somesh, B. P., Sigurdsson, S., Saeki, H., Erdjument-Bromage, H., Tempst, P., & Svejstrup, J. Q. (2007). Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD. Cell, 129(1), 57-68. https://doi.org/10.1016/j.cell.2007.01.046

Vancouver

Somesh BP, Sigurdsson S, Saeki H, Erdjument-Bromage H, Tempst P, Svejstrup JQ. Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD. Cell. 2007 apr. 6;129(1):57-68. https://doi.org/10.1016/j.cell.2007.01.046

Author

Somesh, Baggavalli P. ; Sigurdsson, Stefan ; Saeki, Hideaki ; Erdjument-Bromage, Hediye ; Tempst, Paul ; Svejstrup, Jesper Q. / Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD. I: Cell. 2007 ; Bind 129, Nr. 1. s. 57-68.

Bibtex

@article{2528605e50c94e938ea1c1d58a0b8443,
title = "Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD",
abstract = "Transcriptional arrest triggers ubiquitylation of RNA polymerase II (RNAPII). We mapped the yeast RNAPII ubiquitylation sites and found that they play an important role in elongation and the DNA-damage response. One site lies in a protein domain that is unordered in free RNAPII, but ordered in the elongating form, helping explain the preferential ubiquitylation of this form. The other site is >125 {\AA}ngstroms away, yet mutation of either site affects ubiquitylation of the other, in vitro and in vivo. The basis for this remarkable coupling was uncovered: an Rsp5 (E3) dimer assembled on the RNAPII C-terminal domain (CTD). The ubiquitylation sites bind Ubc5 (E2), which in turn binds Rsp5 to allow modification. Evidence for folding of the CTD compatible with this mechanism of communication between distant sites is provided. These data reveal the specificity and mechanism of RNAPII ubiquitylation and demonstrate that E2s can play a crucial role in substrate recognition.",
author = "Somesh, {Baggavalli P.} and Stefan Sigurdsson and Hideaki Saeki and Hediye Erdjument-Bromage and Paul Tempst and Svejstrup, {Jesper Q.}",
note = "Funding Information: This work was supported by grants from Cancer Research UK, the EU, and the Association for International Cancer Research (to J.Q.S.). S.S. was supported by an EMBO long-term fellowship. We thank Rick Young, Jon Huibregtse, Jim Friesen, Aaron Ciechanover, and Nick Proudfoot for kind gifts of strains or plasmids. David Bushnell is thanked for help with the RNAPII structure. Members of the Svejstrup lab, Peter Verrijzer, Helle Ulrich, Jim Haber, and Arnold Kristjuhan are thanked for comments on the manuscript. ",
year = "2007",
month = apr,
day = "6",
doi = "10.1016/j.cell.2007.01.046",
language = "English",
volume = "129",
pages = "57--68",
journal = "Cell",
issn = "0092-8674",
publisher = "Cell Press",
number = "1",

}

RIS

TY - JOUR

T1 - Communication between Distant Sites in RNA Polymerase II through Ubiquitylation Factors and the Polymerase CTD

AU - Somesh, Baggavalli P.

AU - Sigurdsson, Stefan

AU - Saeki, Hideaki

AU - Erdjument-Bromage, Hediye

AU - Tempst, Paul

AU - Svejstrup, Jesper Q.

N1 - Funding Information: This work was supported by grants from Cancer Research UK, the EU, and the Association for International Cancer Research (to J.Q.S.). S.S. was supported by an EMBO long-term fellowship. We thank Rick Young, Jon Huibregtse, Jim Friesen, Aaron Ciechanover, and Nick Proudfoot for kind gifts of strains or plasmids. David Bushnell is thanked for help with the RNAPII structure. Members of the Svejstrup lab, Peter Verrijzer, Helle Ulrich, Jim Haber, and Arnold Kristjuhan are thanked for comments on the manuscript.

PY - 2007/4/6

Y1 - 2007/4/6

N2 - Transcriptional arrest triggers ubiquitylation of RNA polymerase II (RNAPII). We mapped the yeast RNAPII ubiquitylation sites and found that they play an important role in elongation and the DNA-damage response. One site lies in a protein domain that is unordered in free RNAPII, but ordered in the elongating form, helping explain the preferential ubiquitylation of this form. The other site is >125 Ångstroms away, yet mutation of either site affects ubiquitylation of the other, in vitro and in vivo. The basis for this remarkable coupling was uncovered: an Rsp5 (E3) dimer assembled on the RNAPII C-terminal domain (CTD). The ubiquitylation sites bind Ubc5 (E2), which in turn binds Rsp5 to allow modification. Evidence for folding of the CTD compatible with this mechanism of communication between distant sites is provided. These data reveal the specificity and mechanism of RNAPII ubiquitylation and demonstrate that E2s can play a crucial role in substrate recognition.

AB - Transcriptional arrest triggers ubiquitylation of RNA polymerase II (RNAPII). We mapped the yeast RNAPII ubiquitylation sites and found that they play an important role in elongation and the DNA-damage response. One site lies in a protein domain that is unordered in free RNAPII, but ordered in the elongating form, helping explain the preferential ubiquitylation of this form. The other site is >125 Ångstroms away, yet mutation of either site affects ubiquitylation of the other, in vitro and in vivo. The basis for this remarkable coupling was uncovered: an Rsp5 (E3) dimer assembled on the RNAPII C-terminal domain (CTD). The ubiquitylation sites bind Ubc5 (E2), which in turn binds Rsp5 to allow modification. Evidence for folding of the CTD compatible with this mechanism of communication between distant sites is provided. These data reveal the specificity and mechanism of RNAPII ubiquitylation and demonstrate that E2s can play a crucial role in substrate recognition.

U2 - 10.1016/j.cell.2007.01.046

DO - 10.1016/j.cell.2007.01.046

M3 - Journal article

C2 - 17418786

AN - SCOPUS:33947720525

VL - 129

SP - 57

EP - 68

JO - Cell

JF - Cell

SN - 0092-8674

IS - 1

ER -

ID: 331029964