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Global Analysis of the Mitochondrial N-Proteome Identifies a Processing Peptidase Critical for Protein Stability

(2009) CELL. 139(2). p.428-439
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Abstract
Many mitochondrial proteins are synthesized with N-terminal presequences that are removed by specific peptidases. The N-termini of the mature proteins and thus peptidase cleavage sites have only been determined for a small fraction of mitochondrial proteins and yielded a controversial situation for the cleavage site specificity of the major mitochondrial processing peptidase (MPP). We report a global analysis of the N-proteome of yeast mitochondria, revealing the N-termini of 615 different proteins. Significantly more proteins than predicted contained cleavable presequences. We identified the intermediate cleaving peptidase Icp55, which removes an amino acid from a characteristic set of MPP-generated N-termini, solving the controversial situation of MPP specificity and suggesting that Icp55 converts instable intermediates into stable proteins. Our results suggest that Icp55 is critical for stabilization of the mitochondrial proteome and illustrate how the N-proteome can serve as rich source for a systematic analysis of mitochondrial protein targeting, cleavage and turnover.
Keywords
CLEAVAGE, COMPLEX, INHIBITOR, PREDICTION, ESCHERICHIA-COLI, TARGETING PEPTIDES, AMINOPEPTIDASE-P, END RULE, SEQUENCES, MECHANISM

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Citation

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Chicago
Vogtle, FN, S Wortelkamp, RP Zahedi, D Becker, C Leidhold, Kris Gevaert, J Kellermann, et al. 2009. “Global Analysis of the Mitochondrial N-Proteome Identifies a Processing Peptidase Critical for Protein Stability.” Cell 139 (2): 428–439.
APA
Vogtle, F., Wortelkamp, S., Zahedi, R., Becker, D., Leidhold, C., Gevaert, K., Kellermann, J., et al. (2009). Global Analysis of the Mitochondrial N-Proteome Identifies a Processing Peptidase Critical for Protein Stability. CELL, 139(2), 428–439.
Vancouver
1.
Vogtle F, Wortelkamp S, Zahedi R, Becker D, Leidhold C, Gevaert K, et al. Global Analysis of the Mitochondrial N-Proteome Identifies a Processing Peptidase Critical for Protein Stability. CELL. CAMBRIDGE: CELL PRESS; 2009;139(2):428–39.
MLA
Vogtle, FN, S Wortelkamp, RP Zahedi, et al. “Global Analysis of the Mitochondrial N-Proteome Identifies a Processing Peptidase Critical for Protein Stability.” CELL 139.2 (2009): 428–439. Print.
@article{783112,
  abstract     = {Many mitochondrial proteins are synthesized with N-terminal presequences that are removed by specific peptidases. The N-termini of the mature proteins and thus peptidase cleavage sites have only been determined for a small fraction of mitochondrial proteins and yielded a controversial situation for the cleavage site specificity of the major mitochondrial processing peptidase (MPP). We report a global analysis of the N-proteome of yeast mitochondria, revealing the N-termini of 615 different proteins. Significantly more proteins than predicted contained cleavable presequences. We identified the intermediate cleaving peptidase Icp55, which removes an amino acid from a characteristic set of MPP-generated N-termini, solving the controversial situation of MPP specificity and suggesting that Icp55 converts instable intermediates into stable proteins. Our results suggest that Icp55 is critical for stabilization of the mitochondrial proteome and illustrate how the N-proteome can serve as rich source for a systematic analysis of mitochondrial protein targeting, cleavage and turnover.},
  author       = {Vogtle, FN and Wortelkamp, S and Zahedi, RP and Becker, D and Leidhold, C and Gevaert, Kris and Kellermann, J and Voos, W and Sickmann, A and Pfanner, N and Meisinger, C},
  issn         = {0092-8674},
  journal      = {CELL},
  keyword      = {CLEAVAGE,COMPLEX,INHIBITOR,PREDICTION,ESCHERICHIA-COLI,TARGETING PEPTIDES,AMINOPEPTIDASE-P,END RULE,SEQUENCES,MECHANISM},
  language     = {eng},
  number       = {2},
  pages        = {428--439},
  publisher    = {CELL PRESS},
  title        = {Global Analysis of the Mitochondrial N-Proteome Identifies a Processing Peptidase Critical for Protein Stability},
  url          = {http://dx.doi.org/10.1016/j.cell.2009.07.045},
  volume       = {139},
  year         = {2009},
}

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