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

Shaoping Chen, Joseph A Vetro, Yie Hwa Chang

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

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 gene. We found that MetAP 1 plays the major role in N-terminal methionine removal in yeast. Both MetAPs were less efficient when the second residue was Va1, and MetAP2 was less efficient than MetAP1 when the second residue was Gly, Cys, or Thr. These findings indicate that MetAP1 and MetAP2 exhibit different cleavage efficiencies against the same substrates in vivo. Interestingly, although methionine is considered a stabilizing N-terminal residue, we found that retention of the initiator methionine on the Met-Ala-GST mutant protein drastically reduced its half-life in vivo.

Original languageEnglish (US)
Pages (from-to)87-93
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume398
Issue number1
DOIs
StatePublished - Feb 1 2002

Fingerprint

Aminopeptidases
Methionine
Yeast
Saccharomyces cerevisiae
Glutathione Transferase
Fungal Proteins
Mutant Proteins
Half-Life
Genes
Yeasts
Substrates
Processing
Proteins

Keywords

  • Fumagillin
  • Metalloenzyme
  • Protein processing
  • Protein turnover
  • TNP-470

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

The specificity in vivo of two distinct methionine aminopeptidases in Saccharomyces cerevisiae. / Chen, Shaoping; Vetro, Joseph A; Chang, Yie Hwa.

In: Archives of Biochemistry and Biophysics, Vol. 398, No. 1, 01.02.2002, p. 87-93.

Research output: Contribution to journalArticle

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