PURIFICATION AND CHARACTERIZATION OF AG,ZN-SUPEROXIDE DISMUTASE FROM SACCHAROMYCES-CEREVISIAE EXPOSED TO SILVER

Citation
Mr. Ciriolo et al., PURIFICATION AND CHARACTERIZATION OF AG,ZN-SUPEROXIDE DISMUTASE FROM SACCHAROMYCES-CEREVISIAE EXPOSED TO SILVER, The Journal of biological chemistry, 269(41), 1994, pp. 25783-25787
Citations number
36
Categorie Soggetti
Biology
ISSN journal
00219258
Volume
269
Issue
41
Year of publication
1994
Pages
25783 - 25787
Database
ISI
SICI code
0021-9258(1994)269:41<25783:PACOAD>2.0.ZU;2-#
Abstract
Cu,Zn-superoxide dismutase plays an important role in protecting cells from oxygen toxicity by catalyzing the dismutation of superoxide anio n into hydrogen peroxide and oxygen. In Saccharomyces cerevisiae Cu,Zn -superoxide dismutase is coregulated with copper-thionein by copper vi a the transcription factor ACE 1. We demonstrate here that presence of AgNO(3) in the culture medium leads to a five times increase of Cu,Zn- superoxide dismutase mRNA, with a concomitant six times decrease of th e enzyme activity. Susceptibility of yeast to silver was apparently in versely related to Cu,Zn-superoxide dismutase activity. From silver-tr eated yeast a Cu,Zn-superoxide dismutase with impaired dismutase funct ion was purified and was shown to contain silver, which was located to the copper site. These data suggest that Cu,Zn-superoxide dismutase m ay play an additional direct role in the defense of S. cerevisiae agai nst metal stress by functioning as metal chelator.