The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae.

  title={The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae.},
  author={Shaoping Chen and Joseph A. Vetro and Yie-Hwa Chang},
  journal={Archives of biochemistry and biophysics},
  volume={398 1},
In Saccharomyces cerevisiae, the essential function of amino-terminal methionine removal is provided cotranslationally by two methionine aminopeptidases (MetAP1 and MetAP2). To examine the individual processing efficiency of each MetAP in vivo, we measured the degree of N-terminal methionine cleavage from a series of mutated glutathione-S-transferase (GST) proteins isolated from yeast wild-type, a map1 deletion strain, a map2 deletion strain, and a map1 deletion strain overexpressing the MAP2… 

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  • X. LiY. Chang
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1995
A second methionine aminopeptidase (Met-AP2) is described in Saccharomyces cerevisiae, encoded by MAP2, which was cloned as a suppressor of the slow-growth phenotype of the map1 null strain and was purified by immunoaffinity chromatography and shown to contain Met-AP activity.

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Crude extracts of a multiply peptidase-deficient strain of Salmonella typhimurium contain an aminopeptidase that specifically removes N-terminal methionine from peptides, which suggests that it is involved in the cleavage of meth ionine from newly synthesized peptide chains.

Specificity of cotranslational amino-terminal processing of proteins in yeast.

The results define the specificity of these enzymes in situ and suggest that the nature of the penultimate amino-terminal residue is the major determinant of their selectivity.

Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth

It is suggested that the zinc fingers are essential for normal MAP function in vivo, even though the in vitro enzyme assays indicate that they are not involved in catalysis.

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In vitro analyses with purified enzyme indicated that MAP is a metallo-oligopeptidase with absolute specificity for the amino-terminal methionine, consistent with the deduced specificity of the enzyme based on the analysis of known amino- terminal sequences of intracellular proteins.