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 |
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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) |
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ISSN: | 0014-5793 1873-3468 |
DOI: | 10.1016/0014-5793(89)81734-X |