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Gene Review

MAP1  -  Map1p

Saccharomyces cerevisiae S288c

Synonyms: L9672.12, MAP 1, MetAP 1, Methionine aminopeptidase 1, Peptidase M 1, ...
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Disease relevance of MAP1


High impact information on MAP1

  • Overexpression of HsMetAP1, but not HsMetAP2, conferred resistance of cells to the inhibitors, and the inhibitors caused retention of N-terminal methionine of a known MetAP substrate, suggesting that HsMetAP1 is the cellular target for the inhibitors [2].
  • Transformants of map1 null cells expressing MAP2 in a high-copy-number plasmid contained 3- to 12-fold increases in Met-AP activity on different peptide substrates [3].
  • Overexpression of map1 resulted in enhanced transcription of cell-type-specilic genes, but the range of genes affected by Map1 was restricted by the mating type of the cell [4].
  • Additionally, Gfa1 will be a relevant target in therapeutic or physiological applications in which MetAP activity is inhibited [5].
  • MAP-1 and IAP-1, two novel AAA proteases with catalytic sites on opposite membrane surfaces in mitochondrial inner membrane of Neurospora crassa [6].

Biological context of MAP1

  • Ribosome profiles of map1 null expressing wild-type MetAP1 or one of three zinc finger mutants were compared [7].
  • Results of yeast two-hybrid analysis suggested that Map1 may physically interact with Mat1-Pc, the product of the h(+)-specific mating-type gene mat1-Pc [4].
  • Methionine aminopeptidase (MetAP), in two isoenzymic forms, is responsible for hydrolysis of the initiator methionine residues from the majority of newly synthesized proteins [8].

Anatomical context of MAP1

  • Furthermore, unlike the case for the prokaryotic gene, the deletion of the yeast MAP1 gene is not lethal, suggesting for the first time that alternative NH2-terminal processing pathway(s) exist for cleaving methionine from nascent polypeptide chains in eukaryotic cells [9].

Associations of MAP1 with chemical compounds

  • Limited proteolysis of intact yeast methionine aminopeptidase (MAP1) with trypsin releases a 34 kDa fragment whose NH2-terminal sequence begins at Asp70, immediately following Lys69 [10].
  • In the presence of physiological concentrations of reduced glutathione (GSH), Co-MetAP I is inactive, while the activity of Zn-MetAP I is increased more than 1.7-fold over Zn-MetAP I assayed in the absence of GSH [11].
  • The cis-fumagillin methyl ester, a stereoisomer of fumagillin methyl ester at the C2'-C3' position of the aliphatic side chain, selectively inhibited growth of the map1 mutant yeast strain (MetAP1 deletion strain) at a concentration as low as 1 ng [12].
  • Some of the pyridine-2-carboxylic acid derivatives (compound 2 and 3) had selective inhibition of the growth of map2 deletion yeast and weak inhibition on wild-type yeast growth, while no inhibition on map1 deletion yeast [13].
  • They represent small-molecule MetAP inhibitors with novel structures different from alkylating fumagillin derivatives and peptidic bestatin-based MetAP inhibitor [14].

Regulatory relationships of MAP1

  • 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 [15].

Other interactions of MAP1

  • The map2 null strain, like the map1 null strain, is viable but with a slower growth rate [3].

Analytical, diagnostic and therapeutic context of MAP1


  1. Yeast methionine aminopeptidase I. Alteration of substrate specificity by site-directed mutagenesis. Walker, K.W., Bradshaw, R.A. J. Biol. Chem. (1999) [Pubmed]
  2. Elucidation of the function of type 1 human methionine aminopeptidase during cell cycle progression. Hu, X., Addlagatta, A., Lu, J., Matthews, B.W., Liu, J.O. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  3. Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases. Li, X., Chang, Y.H. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  4. Schizosaccharomyces pombe map1+ encodes a MADS-box-family protein required for cell-type-specific gene expression. Yabana, N., Yamamoto, M. Mol. Cell. Biol. (1996) [Pubmed]
  5. Yeast glutamine-fructose-6-phosphate aminotransferase (Gfa1) requires methionine aminopeptidase activity for proper function. Dummitt, B., Micka, W.S., Chang, Y.H. J. Biol. Chem. (2005) [Pubmed]
  6. MAP-1 and IAP-1, two novel AAA proteases with catalytic sites on opposite membrane surfaces in mitochondrial inner membrane of Neurospora crassa. Klanner, C., Prokisch, H., Langer, T. Mol. Biol. Cell (2001) [Pubmed]
  7. Yeast methionine aminopeptidase type 1 is ribosome-associated and requires its N-terminal zinc finger domain for normal function in vivo. Vetro, J.A., Chang, Y.H. J. Cell. Biochem. (2002) [Pubmed]
  8. Yeast (Saccharomyces cerevisiae) methionine aminopeptidase I: rapid purification and improved activity assay. Walker, K.W., Yi, E., Bradshaw, R.A. Biotechnol. Appl. Biochem. (1999) [Pubmed]
  9. Molecular cloning, sequencing, deletion, and overexpression of a methionine aminopeptidase gene from Saccharomyces cerevisiae. Chang, Y.H., Teichert, U., Smith, J.A. J. Biol. Chem. (1992) [Pubmed]
  10. Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae are important for normal growth. Zuo, S., Guo, Q., Ling, C., Chang, Y.H. Mol. Gen. Genet. (1995) [Pubmed]
  11. Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: a case of mistaken identity? Walker, K.W., Bradshaw, R.A. Protein Sci. (1998) [Pubmed]
  12. cis-fumagillin, a new methionine aminopeptidase (type 2) inhibitor produced by Penicillium sp. F2757. Kwon, J.Y., Jeong, H.W., Kim, H.K., Kang, K.H., Chang, Y.H., Bae, K.S., Choi, J.D., Lee, U.C., Son, K.H., Kwon, B.M. J. Antibiot. (2000) [Pubmed]
  13. Type I methionine aminopeptidase from Saccharomyces cerevisiae is a potential target for antifungal drug screening. Chen, L.L., Li, J., Li, J.Y., Luo, Q.L., Mao, W.F., Shen, Q., Nan, F.J., Ye, Q.Z. Acta Pharmacol. Sin. (2004) [Pubmed]
  14. Discovery and structural modification of inhibitors of methionine aminopeptidases from Escherichia coli and Saccharomyces cerevisiae. Luo, Q.L., Li, J.Y., Liu, Z.Y., Chen, L.L., Li, J., Qian, Z., Shen, Q., Li, Y., Lushington, G.H., Ye, Q.Z., Nan, F.J. J. Med. Chem. (2003) [Pubmed]
  15. Evidence of a dominant negative mutant of yeast methionine aminopeptidase type 2 in Saccharomyces cerevisiae. Vetro, J.A., Dummitt, B., Micka, W.S., Chang, Y.H. J. Cell. Biochem. (2005) [Pubmed]
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