Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome.

Using a genetic strategy designed to find proteins involved in the function of the Saccharomyces cerevisiae transcriptional activator GAL4, we isolated mutants in two genes which rescue a class of gal4 activation domain mutants. One of these genes, SUG1, encodes a member of a large family of putative ATPases, the ...
Conserved ATPase containing Domain (CAD) proteins (also known as AAA proteins) that are involved in a wide variety of cellular functions. Subsequently, SUG1 was identified as a subunit of the 26 S proteasome. We have now cloned the gene defined by the second complementation group. SUG2 encodes an essential 49-kDa protein that is also a member of the CAD family and is 43% identical to SUG1. The mutation in sug2-1, like that in sug1-1, is found in the CAD near the highly conserved ATPase motif. We present biochemical and genetic evidence that SUG2 is associated in vivo with SUG1 and is a novel CAD protein subunit of the 26 S proteasome. With its highly conserved mammalian homologs, human p42 and ground squirrel CADp44, SUG2 defines a new class of proteasomal CAD proteins.
Mesh Terms:
Adenosine Triphosphatases, Amino Acid Sequence, Cysteine Endopeptidases, Fungal Proteins, Genes, Fungal, Genetic Complementation Test, Macromolecular Substances, Molecular Sequence Data, Molecular Weight, Multienzyme Complexes, Mutagenesis, Site-Directed, Proteasome Endopeptidase Complex, Protein Binding, Protein Structure, Secondary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Sequence Homology, Amino Acid, Structure-Activity Relationship
J. Biol. Chem.
Date: Dec. 20, 1996
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