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The Function of Nudix Hydrolase Ysa1 in Saccharomyces cerevisiae
Author(s) -
Tong Lei,
Denu John
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1057.5
Subject(s) - saccharomyces cerevisiae , nad+ kinase , acetylation , biochemistry , biology , transferase , adp ribosylation , chromatin , hydrolase , regulator , enzyme , microbiology and biotechnology , yeast , gene
The silent information regulator 2 (Sir2) family catalyzes NAD + ‐dependent protein deacetylation and functions in the regulation of gene silencing, chromatin structure, and longevity. O ‐acetyl‐ribose ( O AADPr) is a unique product of the Sir2 reaction. In Saccharomyces cerevisiae , we discovered three activities that metabolize O AADPr, an esterase, an acetyl transferase, and a Nudix hydrolase, Ysa1. In vitro , Ysa1 possesses comparable activity towards ADP‐ribose (ADPr) and O AADPr. We compared ADPr/ O AADPr metabolizing activities among the wild type, Ysa1 deletion, and Ysa1 over expression strains. These data suggest that Ysa1 is a major ADPr/ O AADPr metabolizing enzyme in vivo. N ‐acetyl–ADPr analogs were utilized to indicate that O AADPr is directly hydrolyzed by Ysa1, and not through a pathway that first involves conversion of O AADPr to ADPr by the esterase. Using a TAP‐Ysa1 strain and cell fractionation, we localized the TAP signal to mitochondria. We propose that Ysa1 controls ADPr/ O AADPr levels and is important for maintaining mitochrondrial function during cellular stress. Research supported by NIH.