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The Function of Nudix Hydrolase Ysa1 in Saccharomyces cerevisiae
Author(s) -
Tong Lei,
Lee Susan,
Denu John M
Publication year - 2007
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.21.5.a631-a
Subject(s) - saccharomyces cerevisiae , chromatin , biology , gene silencing , histone , acetylation , nad+ kinase , pyrophosphatase , biochemistry , gene , microbiology and biotechnology , enzyme
The Saccharomyces cerevisiae protein Ysa1 belongs to the ADP‐sugar pyrophosphatase subfamily of Nudix hydrolases. In vitro , Ysa1 was shown to possess comparable activity towards ADP‐ribose (ADPr) and the Sir2 reaction product, O ‐acetyl‐ribose ( O AADPr). The silent information regulator 2 (Sir2) family catalyzes NAD‐dependent N‐acetyl‐protein deacetylation and functions in the regulation of gene silencing, chromatin structure, and longevity. 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 . LC/MS/MS are being used to measure cellular levels of ADPr/ O AADPr controlled by Ysa1. The function of Ysa1 is unknown. O AADPr is generated during Saccharomyces cerevisiae histone deacetylation at silent chromatin and was suggested to bind and modulate the structure of the Sir complex; hence Ysa1 could modulate gene silencing via O AADPr degradation. However, deletion or over expression of wild type Ysa1 did not affect silencing at HMR locus. Mistargeting Ysa1 into nuclei by either deletion of the mitochondrial localization sequence, or addition of nuclear localization signal did not show a significant alteration on HMR silencing.