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Title: Alteration of protein synthesis in Saccharomyces cerevisiae caused by transition metals

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:5144869

The effects of transition metals and metal oxides (Co/sup 2 +/, Cu/sup 2 +/, Ni/sup 2 +/, Zn/sup 2 +/, arsenite (AsO/sub 2//sup -/), arsenate (AsO/sub 4//sup 3 -/) and vanadate (VO/sub 4//sup 3 -/)) on protein synthesis and cellular thermotolerance in Saccharomyces cerevisiae have been examined. Arsenate and vanadate differ in that they are known to be physiologic phosphate analogues, e.g. in yeast, arsenate is a competitive inhibitor of phosphate transport and is incorporated into phosphoinositide, while vanadate inhibits the formation of various phosphoproteins and phosphoprotein intermediates. Arsenite and arsenate at concentrations above 0.5 mM and 5 mM, respectively, in minimal glucose media inhibited growth. These two oxides at 1 mM induced 4 of the 6 major heat shock proteins (Hsps): 105, 78, 74 and 36 Kd. The 36 Kd protein as not induced by arsenite at 0.1 mM. Vanadate induced no known Hsp but did induce one polypeptide of 155 Kd. These metal-induced proteins did not confer cellular thermotolerance. No protein induction was observed after 45 min preincubation with 0.5 mM divalent Co, Cu, Ni or Zn despite the fact that as with the metal oxides a significant inhibition of growth and over-all protein synthesis was caused by Co/sup 2 +/, Cu/sup 2 +/ and Ni/sup 2 +/ at that concentration. Thus, among this group of metals the induction of specific proteins appears to be unique to those species which mimic the phosphate group. Stress which alters the growth to cells does not always trigger a specific alteration of protein synthesis.

Research Organization:
State Univ. of New York, Buffalo
OSTI ID:
5144869
Report Number(s):
CONF-8606151-
Journal Information:
Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States), Vol. 45:6; Conference: 76. annual meeting of the Federation of American Society for Experimental Biology, Washington, DC, USA, 8 Jun 1986
Country of Publication:
United States
Language:
English