N α-acetyltransferase deficiency alters protein synthesis in Saccharomyces cerevisiae

Acetylation is the most frequently occurring chemical modification of the α-NH 2 group of eukaryotic proteins and is catalyzed by a N α-acetyltransferase. Two-dimensional gel electrophoresis was used to compare the soluble proteins synthesized in wild type and a mutant ( aaal) yeast cells lacking N...

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Veröffentlicht in:FEBS letters 1989-10, Vol.256 (1), p.139-142
Hauptverfasser: Lee, Fang-Jen S., Lin, Lee-Wen, Smith, John A.
Format: Artikel
Sprache:eng
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Zusammenfassung:Acetylation is the most frequently occurring chemical modification of the α-NH 2 group of eukaryotic proteins and is catalyzed by a N α-acetyltransferase. Two-dimensional gel electrophoresis was used to compare the soluble proteins synthesized in wild type and a mutant ( aaal) yeast cells lacking N α-acetyltransferase. Among 855 soluble proteins identified in wild type and mutant, ~20% of the proteins in the mutant either disappeared or were shifted to higher p I 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 α-acetylation in eukaryotic protein synthesis. Acetyltransferase; Acetylation; (Saccharomyces cerevisiae)
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(89)81734-X