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- W2054455313 abstract "Eukaryotic methionine aminopeptidase type 2 (MetAP2, MetAP2 gene (MAP2)), together with eukaryotic MetAP1, cotranslationally hydrolyzes initiator methionine from nascent polypeptides when the side chain of the second residue is small and uncharged. In this report, we took advantage of the yeast (Saccharomyces cerevisiae) map1 null strain's reliance on MetAP2 activity for the growth and viability to provide evidence of the first dominant negative mutant of eukaryotic MetAP2. Replacement of the conserved His(174) with alanine within the C-terminal catalytic domain of yeast MetAP2 eliminated detectable catalytic activity against a peptide substrate in vitro. Overexpression of MetAP2 (H174A) under the strong GPD promoter in a yeast map1 null strain was lethal, whereas overexpression under the weaker GAL1 promoter slightly inhibited map1 null growth. Deletion mutants further revealed that the N-terminal region of MetAP2 (residues 2-57) is essential but not sufficient for MetAP2 (H174A) to fully interfere with map1 null growth. Together, these results indicate that catalytically inactive MetAP2 is a dominant negative mutant that requires its N-terminal region to interfere with wild-type MetAP2 function." @default.
- W2054455313 created "2016-06-24" @default.
- W2054455313 creator A5008956181 @default.
- W2054455313 creator A5032401659 @default.
- W2054455313 creator A5058262240 @default.
- W2054455313 creator A5091267298 @default.
- W2054455313 date "2005-01-01" @default.
- W2054455313 modified "2023-09-27" @default.
- W2054455313 title "Evidence of a dominant negative mutant of yeast methionine aminopeptidase type 2 inSaccharomyces cerevisiae" @default.
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- W2054455313 doi "https://doi.org/10.1002/jcb.20285" @default.
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