DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro

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Standard

DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro. / Reid, James; Svejstrup, Jesper Q.

I: Journal of Biological Chemistry, Bind 279, Nr. 29, 16.07.2004, s. 29875-29878.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Reid, J & Svejstrup, JQ 2004, 'DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro', Journal of Biological Chemistry, bind 279, nr. 29, s. 29875-29878. https://doi.org/10.1074/jbc.C400185200

APA

Reid, J., & Svejstrup, J. Q. (2004). DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro. Journal of Biological Chemistry, 279(29), 29875-29878. https://doi.org/10.1074/jbc.C400185200

Vancouver

Reid J, Svejstrup JQ. DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro. Journal of Biological Chemistry. 2004 jul. 16;279(29):29875-29878. https://doi.org/10.1074/jbc.C400185200

Author

Reid, James ; Svejstrup, Jesper Q. / DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro. I: Journal of Biological Chemistry. 2004 ; Bind 279, Nr. 29. s. 29875-29878.

Bibtex

@article{dc406647939c46f28692eb055bbd7b67,

title = "DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro",

abstract = "UV-induced DNA damage results in ubiquitylation and degradation of RNA polymerase II (RNAPII). In yeast, this requires the DEF1 gene, the product of which forms a complex with the transcription-coupling repair factor, Rad26. However, whether Defl is directly involved in RNAPII ubiquitylation has remained unclear. Here we report the establishment of a reconstituted system for studying UV-induced RNAPII ubiquitylation, which mimics the known requirements for this process in vitro. Using this system, we show that Defl is indeed directly required for RNAPII ubiquitylation. Moreover, Defl interacts with RNAPII in a damage-dependent manner. These results support a model in which Defl interacts with RNAPII in response to DNA damage, recruiting the ubiquitylation machinery to enable its modification and subsequent degradation.",

author = "James Reid and Svejstrup, {Jesper Q.}",

year = "2004",

month = jul,

day = "16",

doi = "10.1074/jbc.C400185200",

language = "English",

volume = "279",

pages = "29875--29878",

journal = "Journal of Biological Chemistry",

issn = "0021-9258",

publisher = "American Society for Biochemistry and Molecular Biology, Inc.",

number = "29",

}

RIS

TY - JOUR

T1 - DNA damage-induced Def1-RNA polymerase II interaction and Def1 requirement for polymerase ubiquitylation in vitro

AU - Reid, James

AU - Svejstrup, Jesper Q.

PY - 2004/7/16

Y1 - 2004/7/16

N2 - UV-induced DNA damage results in ubiquitylation and degradation of RNA polymerase II (RNAPII). In yeast, this requires the DEF1 gene, the product of which forms a complex with the transcription-coupling repair factor, Rad26. However, whether Defl is directly involved in RNAPII ubiquitylation has remained unclear. Here we report the establishment of a reconstituted system for studying UV-induced RNAPII ubiquitylation, which mimics the known requirements for this process in vitro. Using this system, we show that Defl is indeed directly required for RNAPII ubiquitylation. Moreover, Defl interacts with RNAPII in a damage-dependent manner. These results support a model in which Defl interacts with RNAPII in response to DNA damage, recruiting the ubiquitylation machinery to enable its modification and subsequent degradation.

AB - UV-induced DNA damage results in ubiquitylation and degradation of RNA polymerase II (RNAPII). In yeast, this requires the DEF1 gene, the product of which forms a complex with the transcription-coupling repair factor, Rad26. However, whether Defl is directly involved in RNAPII ubiquitylation has remained unclear. Here we report the establishment of a reconstituted system for studying UV-induced RNAPII ubiquitylation, which mimics the known requirements for this process in vitro. Using this system, we show that Defl is indeed directly required for RNAPII ubiquitylation. Moreover, Defl interacts with RNAPII in a damage-dependent manner. These results support a model in which Defl interacts with RNAPII in response to DNA damage, recruiting the ubiquitylation machinery to enable its modification and subsequent degradation.

U2 - 10.1074/jbc.C400185200

DO - 10.1074/jbc.C400185200

M3 - Journal article

C2 - 15166235

AN - SCOPUS:3142691854

VL - 279

SP - 29875

EP - 29878

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 29

ER -

ID: 331040745