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Wang, W, Chevray, PM and Nathans, D (1996) Mammalian Sug1 and c-Fos in the nuclear 26S proteasome. Proc. Natl. Acad. Sci. U.S.A. 93:8236-40
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.
Adenosine Triphosphatases; Amino Acid Sequence; Animals; Cell Nucleus/enzymology; Cysteine Endopeptidases/chemistry; Fungal Proteins/chemistry; Genetic Complementation Test; Leucine Zippers; Macromolecular Substances; Mice; Molecular Sequence Data; Multienzyme Complexes/chemistry; Nuclear Proteins/chemistry; Nuclear Proteins/genetics; Proteasome Endopeptidase Complex; Proto-Oncogene Proteins c-fos/chemistry; Rats; Repressor Proteins/chemistry; Saccharomyces cerevisiae; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid