Journal article
Rad25 Protein Is Targeted for Degradation by the Ubc4-Ufd4 Pathway
The Journal of biological chemistry, Vol.290(13), pp.8606-8612
03/27/2015
Handle:
https://hdl.handle.net/2376/114457
PMCID: PMC4375509
PMID: 25670855
Abstract
Background:
The proteolytic regulation of DNA repair factors remains poorly understood.
Results:
Six proteins involved in nucleotide excision repair are found to be degraded by the proteasome.
Conclusion:
Rad25 is selected for proteasomal degradation by the Ubc4-Ufd4 pathway.
Significance:
Our results provide novel insights into the role of the proteasome in DNA repair.
Proteasome-mediated proteolysis provides dynamic spatial and temporal modulation of protein concentration in response to various intrinsic and extrinsic challenges. To gain a better understanding of the role of the proteasome in DNA repair, we systematically monitored the stability of 26 proteins involved in nucleotide excision repair (NER) under normal growth conditions. Among six NER factors found to be regulated by the proteasome, we further delineated the specific pathway involved in the degradation of Rad25, a subunit of TFIIH. We demonstrate that Rad25 turnover requires the ubiquitin-conjugating enzyme Ubc4 and the ubiquitin ligase Ufd4. Interestingly, the deletion of
UFD4
specifically suppresses the
rad25
mutant defective in transcription. Our results reveal a novel function of the Ufd4 pathway and another tie between the proteasome and NER regulators.
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Details
- Title
- Rad25 Protein Is Targeted for Degradation by the Ubc4-Ufd4 Pathway
- Creators
- Xin Bao - From theJill L Johnson - theHai Rao - From the
- Publication Details
- The Journal of biological chemistry, Vol.290(13), pp.8606-8612
- Academic Unit
- UNKNOWN
- Publisher
- American Society for Biochemistry and Molecular Biology; 9650 Rockville Pike, Bethesda, MD 20814, U.S.A
- Grant note
- GM 078085 / National Institutes of Health
- Identifiers
- 99900547766001842
- Language
- English
- Resource Type
- Journal article