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Omics assisted N-terminal proteoform and protein expression profiling on methionine aminopeptidase 1 (MetAP1) deletion

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Abstract
Excision of the N-terminal initiator methionine (iMet) residue from nascent peptide chains is an essential and omnipresent protein modification carried out by methionine aminopeptidases (MetAPs) that accounts for a major source of N-terminal proteoform diversity. Although MetAP2 is known to be implicated in processes such as angiogenesis and proliferation in mammals, the physiological role of MetAP1 is much less clear. In this report we studied the omics-wide effects of human MetAP1 deletion and general MetAP inhibition. The levels of iMet retention are inversely correlated with cellular proliferation rates. Further, despite the increased MetAP2 expression on MetAP1 deletion, MetAP2 was unable to restore processing of Met-Ser-, Met-Pro-, and Met-Ala- starting N termini as inferred from the iMet retention profiles observed, indicating a higher activity of MetAP1 over these N termini. Proteome and transcriptome expression profiling point to differential expression of proteins implicated in lipid metabolism, cytoskeleton organization, cell proliferation and protein synthesis upon perturbation of MetAP activity.
Keywords
ESCHERICHIA-COLI, EUKARYOTIC PROTEINS, GENE-EXPRESSION, HUMAN-CELLS, PROTEOMICS, ACETYLTRANSFERASES, QUANTIFICATION, ACETYLATION, YEAST, IDENTIFICATION, SPECIFICITIES, REVEALS

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MLA
Jonckheere, Veronique, et al. “Omics Assisted N-Terminal Proteoform and Protein Expression Profiling on Methionine Aminopeptidase 1 (MetAP1) Deletion.” MOLECULAR & CELLULAR PROTEOMICS, vol. 17, no. 4, 2018, pp. 694–708.
APA
Jonckheere, V., Fijalkowska, D., & Van Damme, P. (2018). Omics assisted N-terminal proteoform and protein expression profiling on methionine aminopeptidase 1 (MetAP1) deletion. MOLECULAR & CELLULAR PROTEOMICS, 17(4), 694–708.
Chicago author-date
Jonckheere, Veronique, Daria Fijalkowska, and Petra Van Damme. 2018. “Omics Assisted N-Terminal Proteoform and Protein Expression Profiling on Methionine Aminopeptidase 1 (MetAP1) Deletion.” MOLECULAR & CELLULAR PROTEOMICS 17 (4): 694–708.
Chicago author-date (all authors)
Jonckheere, Veronique, Daria Fijalkowska, and Petra Van Damme. 2018. “Omics Assisted N-Terminal Proteoform and Protein Expression Profiling on Methionine Aminopeptidase 1 (MetAP1) Deletion.” MOLECULAR & CELLULAR PROTEOMICS 17 (4): 694–708.
Vancouver
1.
Jonckheere V, Fijalkowska D, Van Damme P. Omics assisted N-terminal proteoform and protein expression profiling on methionine aminopeptidase 1 (MetAP1) deletion. MOLECULAR & CELLULAR PROTEOMICS. 2018;17(4):694–708.
IEEE
[1]
V. Jonckheere, D. Fijalkowska, and P. Van Damme, “Omics assisted N-terminal proteoform and protein expression profiling on methionine aminopeptidase 1 (MetAP1) deletion,” MOLECULAR & CELLULAR PROTEOMICS, vol. 17, no. 4, pp. 694–708, 2018.
@article{8553814,
  abstract     = {Excision of the N-terminal initiator methionine (iMet) residue from nascent peptide chains is an essential and omnipresent protein modification carried out by methionine aminopeptidases (MetAPs) that accounts for a major source of N-terminal proteoform diversity. Although MetAP2 is known to be implicated in processes such as angiogenesis and proliferation in mammals, the physiological role of MetAP1 is much less clear. In this report we studied the omics-wide effects of human MetAP1 deletion and general MetAP inhibition. The levels of iMet retention are inversely correlated with cellular proliferation rates. Further, despite the increased MetAP2 expression on MetAP1 deletion, MetAP2 was unable to restore processing of Met-Ser-, Met-Pro-, and Met-Ala- starting N termini as inferred from the iMet retention profiles observed, indicating a higher activity of MetAP1 over these N termini. Proteome and transcriptome expression profiling point to differential expression of proteins implicated in lipid metabolism, cytoskeleton organization, cell proliferation and protein synthesis upon perturbation of MetAP activity.},
  author       = {Jonckheere, Veronique and Fijalkowska, Daria and Van Damme, Petra},
  issn         = {1535-9476},
  journal      = {MOLECULAR & CELLULAR PROTEOMICS},
  keywords     = {ESCHERICHIA-COLI,EUKARYOTIC PROTEINS,GENE-EXPRESSION,HUMAN-CELLS,PROTEOMICS,ACETYLTRANSFERASES,QUANTIFICATION,ACETYLATION,YEAST,IDENTIFICATION,SPECIFICITIES,REVEALS},
  language     = {eng},
  number       = {4},
  pages        = {694--708},
  title        = {Omics assisted N-terminal proteoform and protein expression profiling on methionine aminopeptidase 1 (MetAP1) deletion},
  url          = {http://dx.doi.org/10.1074/mcp.ra117.000360},
  volume       = {17},
  year         = {2018},
}

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