Pnc1p supports increases in cellular NAD(H) levels in response to internal or external oxidative stress.
Following transfer from medium with fermentable glucose to medium with nonfermentable acetate as the carbon source, cellular levels of NAD(H) were found to increase approximately 2-fold in a parental yeast strain. Similar transfer of a mutant strain subject to endogenous oxidative stress under these conditions produced more dramatic increases in cellular levels of NAD(H), and elevations above parental levels were shown to be due to the nicotinimidase Pnc1p. Similar transient increases in NAD(H) levels observed in the parental strain following addition of exogenous hydrogen peroxide were also attributable to Pnc1p.
Minard
Karyl I
KI
Department of Biochemistry, University of Texas Health Science Center, San Antonio, TX 77229-3900, USA.
McAlister-Henn
Lee
L
D000085:Acetates / Q000378:metabolism / Q000494:pharmacology; D005285:Fermentation; D005656:Fungal Proteins; D005947:Glucose / Q000378:metabolism; D006861:Hydrogen Peroxide / Q000494:pharmacology; D009243:NAD / Q000032:analysis / Q000378:metabolism*; D009535:Nicotinamidase / Q000378:metabolism*; D018384:Oxidative Stress; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D015003:Yeasts / Q000378:metabolism*
D000085:Acetates; D005656:Fungal Proteins; D029701:Saccharomyces cerevisiae Proteins; D009243:NAD; D006861:Hydrogen Peroxide; D009535:Nicotinamidase; C474330:PNC1 protein, S cerevisiae; D005947:Glucose