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PMID: 12488589 Published · ppublish English Journal Article

Regulation of repair by the 26S proteasome.

Journal of biomedicine & biotechnology ·Vol. 2 ·No. 2 ·2002-00-00 ·Pages 94-105

Sweder K, Madura K

Abstract

Cellular processes such as transcription and DNA repair may be regulated through diverse mechanisms, including RNA synthesis, protein synthesis, posttranslational modification and protein degradation. The 26S proteasome, which is responsible for degrading a broad spectrum of proteins, has been shown to interact with several nucleotide excision repair proteins, including xeroderma pigmentosum B protein (XPB), Rad4, and Rad23. Rad4 and Rad23 form a complex that binds preferentially to UV-damaged DNA. The 26S proteasome may regulate repair by degrading DNA repair proteins after repair is completed or, alternatively, the proteasome may act as a molecular chaperone to promote disassembly of the repair complex. In either case, the interaction between the proteasome and nucleotide excision repair depends on proteins like Rad23 that bind ubiquitin-conjugated proteins and the proteasome. While the iteration between Rad4 and Rad23 is well established, it will be interesting to determine what other proteins are regulated in a Rad23-dependent manner.

Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sweder K.
Madura K.
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Article Info
Journal
Journal of biomedicine & biotechnology
Abbr.
J Biomed Biotechnol
ISSN
1110-7251
DOI
10.1155/S1110724302205033
Published
2002-00-00
Pages
94-105
Language
English
Region
United States
NLM ID
101135740
PMCID
PMC153791
Grants
NCI NIH HHS · R01 CA083875 · United States
External Links
PubMed source DOI: 10.1155/S1110724302205033 PMC Full Text
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