Regulation of repair by the 26S proteasome
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...
| Main Authors: | , |
|---|---|
| Format: | Article |
| Language: | English |
| Published: |
Hindawi Limited
2002-01-01
|
| Series: | Journal of Biomedicine and Biotechnology |
| Online Access: | http://dx.doi.org/10.1155/S1110724302205033 |
| Summary: | 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. |
|---|---|
| ISSN: | 1110-7243 1110-7251 |