Journal article
Rad23 Provides a Link between the Png1 Deglycosylating Enzyme and the 26 S Proteasome in Yeast
The Journal of biological chemistry, Vol.276(24), pp.21601-21607
06/15/2001
DOI: 10.1074/jbc.M100826200
PMID: 11259433
Abstract
In addition to a role in DNA repair events in yeast, several lines of evidence indicate that the Rad23 protein (Rad23p) may regulate the activity of the 26 S proteasome. We report evidence that a de-N-glycosylating enzyme, Png1p, may be involved in the proteasomal degradation pathway via its binding to Rad23p. Interaction of Rad23p and Png1p was first detected by two-hybrid screening, and this interaction in vivo was confirmed by biochemical analyses. The Png1p-Rad23p complex was shown to be distinct from the well established DNA repair complex, Rad4p-Rad23p. We propose a model in which Rad23p functions as an escort protein to link the 26 S proteasome with proteins such as Rad4p or Png1p to regulate their cellular activities.
Details
- Title: Subtitle
- Rad23 Provides a Link between the Png1 Deglycosylating Enzyme and the 26 S Proteasome in Yeast
- Creators
- Tadashi Suzuki - Stony Brook UniversityHangil Park - Stony Brook UniversityMichael A. Kwofie - Stony Brook UniversityWilliam J. Lennarz - Stony Brook University
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.276(24), pp.21601-21607
- DOI
- 10.1074/jbc.M100826200
- PMID
- 11259433
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 06/15/2001
- Academic Unit
- Radiology
- Record Identifier
- 9984318819502771
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