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Russell, SJ, Sathyanarayana, UG and Johnston, SA (1996) Isolation and characterization of SUG2. A novel ATPase family component of the yeast 26 S proteasome. J. Biol. Chem. 271:32810-7


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.




Adenosine Triphosphatases/genetics; Adenosine Triphosphatases/isolation & purification; Adenosine Triphosphatases/ultrastructure; Amino Acid Sequence; Cysteine Endopeptidases/chemistry; Cysteine Endopeptidases/genetics; Cysteine Endopeptidases/isolation & purification; Fungal Proteins/genetics; Fungal Proteins/isolation & purification; Genes, Fungal; Genetic Complementation Test; Macromolecular Substances; Molecular Sequence Data; Molecular Weight; Multienzyme Complexes/chemistry; Multienzyme Complexes/genetics; Multienzyme Complexes/isolation & purification; Mutagenesis, Site-Directed; Proteasome Endopeptidase Complex; Protein Binding; Protein Structure, Secondary; Saccharomyces cerevisiae/enzymology; Saccharomyces cerevisiae Proteins; Sequence Alignment; Sequence Homology, Amino Acid; Structure-Activity Relationship