Rescue of arrested RNA polymerase II complexes

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Standard

Rescue of arrested RNA polymerase II complexes. / Svejstrup, Jesper Q.

I: Journal of Cell Science, Bind 116, Nr. 3, 01.02.2003, s. 447-451.

Publikation: Bidrag til tidsskrift › Review › Forskning › fagfællebedømt

Harvard

Svejstrup, JQ 2003, 'Rescue of arrested RNA polymerase II complexes', Journal of Cell Science, bind 116, nr. 3, s. 447-451. https://doi.org/10.1242/jcs.00271

APA

Svejstrup, J. Q. (2003). Rescue of arrested RNA polymerase II complexes. Journal of Cell Science, 116(3), 447-451. https://doi.org/10.1242/jcs.00271

Vancouver

Svejstrup JQ. Rescue of arrested RNA polymerase II complexes. Journal of Cell Science. 2003 feb. 1;116(3):447-451. https://doi.org/10.1242/jcs.00271

Author

Svejstrup, Jesper Q. / Rescue of arrested RNA polymerase II complexes. I: Journal of Cell Science. 2003 ; Bind 116, Nr. 3. s. 447-451.

Bibtex

@article{424d02ec50ba46e6af4fcf1af7ccb21d,
title = "Rescue of arrested RNA polymerase II complexes",
abstract = "In the past few months, several discoveries relating to the mechanism underlying transcription-coupled DNA repair (TCR) have been reported. These results make it timely to propose a hypothesis for how eukaryotic cells might deal with arrested RNA polymerase II (Pol II) complexes. In this model, the transcription-repair coupling factor Cockayne Syndrome B (or the yeast equivalent Rad26) uses DNA translocase activity to remodel the Pol II-DNA interface, possibly to push the polymerase past the obstruction or to remove it from the DNA so that repair can take place if the obstacle is a DNA lesion. However, when this action is not possible and Pol II is left irreversibly trapped on DNA, the polymerase is instead ubiquitylated and eventually removed by proteolysis.",
keywords = "Cockayne syndrome, Def1, RNA polymerase II, Swi/Snf, Transcript elongation, Transcription-coupled repair, Ubiquitylation",
author = "Svejstrup, {Jesper Q.}",
year = "2003",
month = feb,
day = "1",
doi = "10.1242/jcs.00271",
language = "English",
volume = "116",
pages = "447--451",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "The/Company of Biologists Ltd.",
number = "3",

}

RIS

TY - JOUR

T1 - Rescue of arrested RNA polymerase II complexes

AU - Svejstrup, Jesper Q.

PY - 2003/2/1

Y1 - 2003/2/1

N2 - In the past few months, several discoveries relating to the mechanism underlying transcription-coupled DNA repair (TCR) have been reported. These results make it timely to propose a hypothesis for how eukaryotic cells might deal with arrested RNA polymerase II (Pol II) complexes. In this model, the transcription-repair coupling factor Cockayne Syndrome B (or the yeast equivalent Rad26) uses DNA translocase activity to remodel the Pol II-DNA interface, possibly to push the polymerase past the obstruction or to remove it from the DNA so that repair can take place if the obstacle is a DNA lesion. However, when this action is not possible and Pol II is left irreversibly trapped on DNA, the polymerase is instead ubiquitylated and eventually removed by proteolysis.

AB - In the past few months, several discoveries relating to the mechanism underlying transcription-coupled DNA repair (TCR) have been reported. These results make it timely to propose a hypothesis for how eukaryotic cells might deal with arrested RNA polymerase II (Pol II) complexes. In this model, the transcription-repair coupling factor Cockayne Syndrome B (or the yeast equivalent Rad26) uses DNA translocase activity to remodel the Pol II-DNA interface, possibly to push the polymerase past the obstruction or to remove it from the DNA so that repair can take place if the obstacle is a DNA lesion. However, when this action is not possible and Pol II is left irreversibly trapped on DNA, the polymerase is instead ubiquitylated and eventually removed by proteolysis.

KW - Cockayne syndrome

KW - Def1

KW - RNA polymerase II

KW - Swi/Snf

KW - Transcript elongation

KW - Transcription-coupled repair

KW - Ubiquitylation

U2 - 10.1242/jcs.00271

DO - 10.1242/jcs.00271

M3 - Review

C2 - 12508106

AN - SCOPUS:0037326318

VL - 116

SP - 447

EP - 451

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - 3

ER -

ID: 331041682