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Mammalian Sug1 and c-Fos in the nuclear 26S proteasome.

Authors: Wang, W  Chevray, PM  Nathans, D 
Citation: Wang W, etal., Proc Natl Acad Sci U S A. 1996 Aug 6;93(16):8236-40.
Pubmed: (View Article at PubMed) PMID:8710853

In a search for regulatory proteins that interact with the leucine zipper motif of c-Fos in the yeast two-hybrid screen, we have identified a protein (FZA-B) that has extensive sequence similarity to SUG1 of Saccharomyces cerevisiae. Here we show that FZA-B can functionally substitute for SUG1 in yeast and that FZA-B interacts with Fos proteins in vitro through their leucine zippers. In rat liver and in HeLa cells, FZA-B is present in the 26S proteasome complex, as is c-Fos. Immobilized antibody raised against an FZA-B-specific peptide depleted peptidase activity, proteasomal proteins, FZA-B, and c-Fos from a 26S proteasome preparation. FZA-B is found predominantly in the nuclear fraction of COS cells expressing an FZA-B transgene and in the nuclear 26S proteasome of HeLa cells. We conclude that FZA-B is the mammalian homolog of SUG1 (mSug1) and that it is present in the nuclear 26S proteasome of cells. Our results suggest that mSug1 may be involved in the degradation of c-Fos and other transcription factors.

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CRRD Object Information
CRRD ID: 6771234
Created: 2012-07-24
Species: All species
Last Modified: 2012-07-24
Status: ACTIVE



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