N alpha-acetyltransferase deficiency alters protein synthesis in Saccharomyces cerevisiae.
Acetylation is the most frequently occurring chemical modification of the alpha-NH2 group of eukaryotic proteins and is catalyzed by a N alpha-acetyltransferase. Two-dimensional gel electrophoresis was used to compare the soluble proteins synthesized in wild type and a mutant (aaa1) yeast cells lacking N alpha-acetyltransferase. Among 855 soluble proteins identified in wild type and mutant, approximately 20% of the proteins in the mutant either disappeared or were shifted to higher pI without a change of molecular mass, and 27 proteins were observed only in the mutant. In addition, the synthesis of another 12% of the proteins in the mutant was either diminished or enhanced, suggesting that the acetylation of certain regulatory proteins may affect their expression. This is the first demonstration of the broad-based functional role of N alpha-acetylation in eukaryotic protein synthesis.
Lee
F J
FJ
Department of Molecular Biology, Massachusetts General Hospital, Boston.
Lin
L W
LW
Smith
J A
JA
D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism*; D001191:Arylamine N-Acetyltransferase / Q000235:genetics / Q000378:metabolism*; D002384:Catalysis; D003201:Computers; D015180:Electrophoresis, Gel, Two-Dimensional; D005656:Fungal Proteins / Q000096:biosynthesis* / Q000235:genetics; D008715:Methionine / Q000032:analysis; D009154:Mutation; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D012995:Solubility
D005656:Fungal Proteins; D008715:Methionine; D000123:Acetyltransferases; D001191:Arylamine N-Acetyltransferase