Open AccessRub1p Processing by Yuh1p Is Required for Wild-Type Levels of Rub1p Conjugation to Cdc53p
Author(s) -
Bolan Linghu,
Judy Callis,
Mark G. Goebl
Publication year - 2002
Publication title -
eukaryotic cell
Language(s) - English
Resource type - Journals
eISSN - 1535-9778
pISSN - 1535-9786
DOI - 10.1128/ec.1.3.491-494.2002
Subject(s) - asparagine , conjugated system , residue (chemistry) , biochemistry , enzyme , saccharomyces cerevisiae , biology , ubiquitin , yeast , chemistry , gene , polymer , organic chemistry
In Saccharomyces cerevisiae, Rub1p, like ubiquitin, is conjugated to proteins. Before protein conjugation, the carboxyl-terminal asparagine residue of Rub1p is removed. Rub1p conjugation is dependent on the carboxyl-terminal processing enzyme Yuh1p, whereas Rub1p lacking the asparagine residue is conjugated without Yuh1p. Thus, Yuh1p is the major processing enzyme for Rub1p.
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