Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.

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Standard

Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. / Weems, JC; Slaughter, BD; Unruh, JR; Boeing, S; Hall, SM; McLaird, MB; Yasukawa, T; Aso, T; Svejstrup, JQ; Conaway, JW; Conaway, RC.

I: The Journal of Biological Chemistry, Bind 292, Nr. 16, 2017, s. 6431-6437.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Weems, JC, Slaughter, BD, Unruh, JR, Boeing, S, Hall, SM, McLaird, MB, Yasukawa, T, Aso, T, Svejstrup, JQ, Conaway, JW & Conaway, RC 2017, 'Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.', The Journal of Biological Chemistry, bind 292, nr. 16, s. 6431-6437. https://doi.org/10.1074/jbc.C117.777946

APA

Weems, JC., Slaughter, BD., Unruh, JR., Boeing, S., Hall, SM., McLaird, MB., Yasukawa, T., Aso, T., Svejstrup, JQ., Conaway, JW., & Conaway, RC. (2017). Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. The Journal of Biological Chemistry, 292(16), 6431-6437. https://doi.org/10.1074/jbc.C117.777946

Vancouver

Weems JC, Slaughter BD, Unruh JR, Boeing S, Hall SM, McLaird MB o.a. Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. The Journal of Biological Chemistry. 2017;292(16):6431-6437. https://doi.org/10.1074/jbc.C117.777946

Author

Weems, JC ; Slaughter, BD ; Unruh, JR ; Boeing, S ; Hall, SM ; McLaird, MB ; Yasukawa, T ; Aso, T ; Svejstrup, JQ ; Conaway, JW ; Conaway, RC. / Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. I: The Journal of Biological Chemistry. 2017 ; Bind 292, Nr. 16. s. 6431-6437.

Bibtex

@article{5515ec6b9d49493b8625332dc719fdf2,
title = "Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.",
abstract = "Elongin A performs dual functions as the transcriptionally active subunit of RNA polymerase II (Pol II) elongation factor Elongin and as the substrate recognition subunit of a Cullin-RING E3 ubiquitin ligase that ubiquitylates Pol II in response to DNA damage. Assembly of the Elongin A ubiquitin ligase and its recruitment to sites of DNA damage is a tightly regulated process induced by DNA-damaging agents and α-amanitin, a drug that induces Pol II stalling. In this study, we demonstrate (i) that Elongin A and the ubiquitin ligase subunit CUL5 associate in cells with the Cockayne syndrome B (CSB) protein and (ii) that this interaction is also induced by DNA-damaging agents and α-amanitin. In addition, we present evidence that the CSB protein promotes stable recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. Our findings are consistent with the model that the Elongin A ubiquitin ligase and the CSB protein function together in a common pathway in response to Pol II stalling and DNA damage.",
author = "JC Weems and BD Slaughter and JR Unruh and S Boeing and SM Hall and MB McLaird and T Yasukawa and T Aso and JQ Svejstrup and JW Conaway and RC Conaway",
year = "2017",
doi = "10.1074/jbc.C117.777946",
language = "English",
volume = "292",
pages = "6431--6437",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology, Inc.",
number = "16",

}

RIS

TY - JOUR

T1 - Cockayne syndrome B protein regulates recruitment of the Elongin A ubiquitin ligase to sites of DNA damage.

AU - Weems, JC

AU - Slaughter, BD

AU - Unruh, JR

AU - Boeing, S

AU - Hall, SM

AU - McLaird, MB

AU - Yasukawa, T

AU - Aso, T

AU - Svejstrup, JQ

AU - Conaway, JW

AU - Conaway, RC

PY - 2017

Y1 - 2017

N2 - Elongin A performs dual functions as the transcriptionally active subunit of RNA polymerase II (Pol II) elongation factor Elongin and as the substrate recognition subunit of a Cullin-RING E3 ubiquitin ligase that ubiquitylates Pol II in response to DNA damage. Assembly of the Elongin A ubiquitin ligase and its recruitment to sites of DNA damage is a tightly regulated process induced by DNA-damaging agents and α-amanitin, a drug that induces Pol II stalling. In this study, we demonstrate (i) that Elongin A and the ubiquitin ligase subunit CUL5 associate in cells with the Cockayne syndrome B (CSB) protein and (ii) that this interaction is also induced by DNA-damaging agents and α-amanitin. In addition, we present evidence that the CSB protein promotes stable recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. Our findings are consistent with the model that the Elongin A ubiquitin ligase and the CSB protein function together in a common pathway in response to Pol II stalling and DNA damage.

AB - Elongin A performs dual functions as the transcriptionally active subunit of RNA polymerase II (Pol II) elongation factor Elongin and as the substrate recognition subunit of a Cullin-RING E3 ubiquitin ligase that ubiquitylates Pol II in response to DNA damage. Assembly of the Elongin A ubiquitin ligase and its recruitment to sites of DNA damage is a tightly regulated process induced by DNA-damaging agents and α-amanitin, a drug that induces Pol II stalling. In this study, we demonstrate (i) that Elongin A and the ubiquitin ligase subunit CUL5 associate in cells with the Cockayne syndrome B (CSB) protein and (ii) that this interaction is also induced by DNA-damaging agents and α-amanitin. In addition, we present evidence that the CSB protein promotes stable recruitment of the Elongin A ubiquitin ligase to sites of DNA damage. Our findings are consistent with the model that the Elongin A ubiquitin ligase and the CSB protein function together in a common pathway in response to Pol II stalling and DNA damage.

U2 - 10.1074/jbc.C117.777946

DO - 10.1074/jbc.C117.777946

M3 - Journal article

C2 - 28292928

VL - 292

SP - 6431

EP - 6437

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 16

ER -

ID: 331083250