Journal article
Yeast Deubiquitinase Ubp3 Interacts with the 26 S Proteasome to Facilitate Rad4 Degradation
The Journal of biological chemistry, Vol.285(48), pp.37542-37550
11/26/2010
Handle:
https://hdl.handle.net/2376/114274
PMCID: PMC2988359
PMID: 20876584
Abstract
Deubiquitinating enzymes (DUBs) function in a variety of cellular processes by removing ubiquitin moieties from substrates, but their role in DNA repair has not been elucidated. Yeast Rad4-Rad23 heterodimer is responsible for recognizing DNA damage in nucleotide excision repair (NER). Rad4 binds to UV damage directly while Rad23 stabilizes Rad4 from proteasomal degradation. Here, we show that disruption of yeast deubiquitinase
UBP3
leads to enhanced UV resistance, increased repair of UV damage and Rad4 levels in
rad23
Δ cells, and elevated Rad4 stability. A catalytically inactive Ubp3 (Ubp3-C469A), however, is unable to affect NER or Rad4. Consistent with its role in down-regulating Rad4, Ubp3 physically interacts with Rad4 and the proteasome, both
in vivo
and
in vitro
, suggesting that Ubp3 associates with the proteasome to facilitate Rad4 degradation and thus suppresses NER.
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Details
- Title
- Yeast Deubiquitinase Ubp3 Interacts with the 26 S Proteasome to Facilitate Rad4 Degradation
- Creators
- Peng Mao - From Biochemistry and Biophysics, School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-7520Michael J Smerdon - From Biochemistry and Biophysics, School of Molecular Biosciences, Washington State University, Pullman, Washington 99164-7520
- Publication Details
- The Journal of biological chemistry, Vol.285(48), pp.37542-37550
- Academic Unit
- Molecular Biosciences, School of
- Publisher
- American Society for Biochemistry and Molecular Biology; 9650 Rockville Pike, Bethesda, MD 20814, U.S.A
- Grant note
- ES002614 / National Institutes of Health
- Identifiers
- 99900548376001842
- Language
- English
- Resource Type
- Journal article