Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation

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Standard

Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. / Harreman, Michelle; Taschner, Michael; Sigurdsson, Stefan; Anindya, Roy; Reid, James; Somesh, Baggavalli; Kong, Stephanie E.; Banks, Charles A.S.; Conaway, Ronald C.; Conaway, Joan W.; Svejstrup, Jesper Q.

I: Proceedings of the National Academy of Sciences of the United States of America, Bind 106, Nr. 49, 08.12.2009, s. 20705-20710.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Harreman, M, Taschner, M, Sigurdsson, S, Anindya, R, Reid, J, Somesh, B, Kong, SE, Banks, CAS, Conaway, RC, Conaway, JW & Svejstrup, JQ 2009, 'Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation', Proceedings of the National Academy of Sciences of the United States of America, bind 106, nr. 49, s. 20705-20710. https://doi.org/10.1073/pnas.0907052106

APA

Harreman, M., Taschner, M., Sigurdsson, S., Anindya, R., Reid, J., Somesh, B., Kong, S. E., Banks, C. A. S., Conaway, R. C., Conaway, J. W., & Svejstrup, J. Q. (2009). Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proceedings of the National Academy of Sciences of the United States of America, 106(49), 20705-20710. https://doi.org/10.1073/pnas.0907052106

Vancouver

Harreman M, Taschner M, Sigurdsson S, Anindya R, Reid J, Somesh B o.a. Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. Proceedings of the National Academy of Sciences of the United States of America. 2009 dec. 8;106(49):20705-20710. https://doi.org/10.1073/pnas.0907052106

Author

Harreman, Michelle ; Taschner, Michael ; Sigurdsson, Stefan ; Anindya, Roy ; Reid, James ; Somesh, Baggavalli ; Kong, Stephanie E. ; Banks, Charles A.S. ; Conaway, Ronald C. ; Conaway, Joan W. ; Svejstrup, Jesper Q. / Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation. I: Proceedings of the National Academy of Sciences of the United States of America. 2009 ; Bind 106, Nr. 49. s. 20705-20710.

Bibtex

@article{a6497814890c4abbbbbdc8d308a99b30,
title = "Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation",
abstract = "The proteasome degrades proteins modified by polyubiquitylation, so correctly controlled ubiquitylation is crucial to avoid unscheduled proteolysis of essential proteins. The mechanism regulating proteolysis of RNAPII has been controversial since two distinct ubiquitin ligases (E3s), Rsp5 (and its human homologue NEDD4) and Elongin-Cullin complex, have both been shown to be required for its DNA-damage-induced polyubiquitylation. Here we show that these E3s work sequentially in a two-step mechanism. First, Rsp5 adds mono-ubiquitin, or sometimes a ubiquitin chain linked via ubiquitin lysine 63 that does not trigger proteolysis. When produced, the K63 chain can be trimmed to mono-ubiquitylation by an Rsp5-associated ubiquitin protease, Ubp2. Based on this mono-ubiquitin moiety on RNAPII, an Elc1/Cul3 complex then produces a ubiquitin chain linked via lysine 48, which can trigger proteolysis. Likewise, for correct polyubiquitylation of human RNAPII, NEDD4 cooperates with the ElonginA/B/C-Cullin 5 complex. These data indicate that RNAPII polyubiquitylation requires cooperation between distinct, sequentially acting ubiquitin ligases, and raise the intriguing possibility that other members of the large and functionally diverse family of NEDD4-like ubiquitin ligases also require the assistance of a second E3 when targeting proteins for degradation.",
keywords = "Elongin, NEDD4, Rsp5, Ubiquitylation",
author = "Michelle Harreman and Michael Taschner and Stefan Sigurdsson and Roy Anindya and James Reid and Baggavalli Somesh and Kong, {Stephanie E.} and Banks, {Charles A.S.} and Conaway, {Ronald C.} and Conaway, {Joan W.} and Svejstrup, {Jesper Q.}",
year = "2009",
month = dec,
day = "8",
doi = "10.1073/pnas.0907052106",
language = "English",
volume = "106",
pages = "20705--20710",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
publisher = "The National Academy of Sciences of the United States of America",
number = "49",

}

RIS

TY - JOUR

T1 - Distinct ubiquitin ligases act sequentially for RNA polymerase II polyubiquitylation

AU - Harreman, Michelle

AU - Taschner, Michael

AU - Sigurdsson, Stefan

AU - Anindya, Roy

AU - Reid, James

AU - Somesh, Baggavalli

AU - Kong, Stephanie E.

AU - Banks, Charles A.S.

AU - Conaway, Ronald C.

AU - Conaway, Joan W.

AU - Svejstrup, Jesper Q.

PY - 2009/12/8

Y1 - 2009/12/8

N2 - The proteasome degrades proteins modified by polyubiquitylation, so correctly controlled ubiquitylation is crucial to avoid unscheduled proteolysis of essential proteins. The mechanism regulating proteolysis of RNAPII has been controversial since two distinct ubiquitin ligases (E3s), Rsp5 (and its human homologue NEDD4) and Elongin-Cullin complex, have both been shown to be required for its DNA-damage-induced polyubiquitylation. Here we show that these E3s work sequentially in a two-step mechanism. First, Rsp5 adds mono-ubiquitin, or sometimes a ubiquitin chain linked via ubiquitin lysine 63 that does not trigger proteolysis. When produced, the K63 chain can be trimmed to mono-ubiquitylation by an Rsp5-associated ubiquitin protease, Ubp2. Based on this mono-ubiquitin moiety on RNAPII, an Elc1/Cul3 complex then produces a ubiquitin chain linked via lysine 48, which can trigger proteolysis. Likewise, for correct polyubiquitylation of human RNAPII, NEDD4 cooperates with the ElonginA/B/C-Cullin 5 complex. These data indicate that RNAPII polyubiquitylation requires cooperation between distinct, sequentially acting ubiquitin ligases, and raise the intriguing possibility that other members of the large and functionally diverse family of NEDD4-like ubiquitin ligases also require the assistance of a second E3 when targeting proteins for degradation.

AB - The proteasome degrades proteins modified by polyubiquitylation, so correctly controlled ubiquitylation is crucial to avoid unscheduled proteolysis of essential proteins. The mechanism regulating proteolysis of RNAPII has been controversial since two distinct ubiquitin ligases (E3s), Rsp5 (and its human homologue NEDD4) and Elongin-Cullin complex, have both been shown to be required for its DNA-damage-induced polyubiquitylation. Here we show that these E3s work sequentially in a two-step mechanism. First, Rsp5 adds mono-ubiquitin, or sometimes a ubiquitin chain linked via ubiquitin lysine 63 that does not trigger proteolysis. When produced, the K63 chain can be trimmed to mono-ubiquitylation by an Rsp5-associated ubiquitin protease, Ubp2. Based on this mono-ubiquitin moiety on RNAPII, an Elc1/Cul3 complex then produces a ubiquitin chain linked via lysine 48, which can trigger proteolysis. Likewise, for correct polyubiquitylation of human RNAPII, NEDD4 cooperates with the ElonginA/B/C-Cullin 5 complex. These data indicate that RNAPII polyubiquitylation requires cooperation between distinct, sequentially acting ubiquitin ligases, and raise the intriguing possibility that other members of the large and functionally diverse family of NEDD4-like ubiquitin ligases also require the assistance of a second E3 when targeting proteins for degradation.

KW - Elongin

KW - NEDD4

KW - Rsp5

KW - Ubiquitylation

U2 - 10.1073/pnas.0907052106

DO - 10.1073/pnas.0907052106

M3 - Journal article

C2 - 19920177

AN - SCOPUS:73949101221

VL - 106

SP - 20705

EP - 20710

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 49

ER -

ID: 330994330