Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing

Z. N. Karamysheva, A. L. Karamyshev, V. N. Ksenzenko, M. G. Shlyapnikov, A. V. Kayawa, M. A. Nesmeyanova

Research output: Contribution to journalArticle

Abstract

The effect of 57 amino acid substitutions in the C-proximal domain of the Esherichia coli alkaline phosphatase signal peptide on the processing of this protein was studied. Only substitution of aromatic (Phe, Tyr), charged (Lys, His, Glu), or highly polar amino acids into positions -1 and -3, or introduction of Pro at -3 and Leu at -1 completely interrupt processing. The results are a new experimental demonstration of the "-3, -1" rule that describes the processing sites of secreted proteins. It is shown for the first time that the processing efficiency is also determined by the structure of amino acids in positions -2 and -5.

Original languageEnglish (US)
Pages (from-to)768-774
Number of pages7
JournalMolecular Biology
Volume31
Issue number5
StatePublished - Sep 1 1997

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Keywords

  • Alkaline phosphatase
  • Amino acid substitutions
  • Biogenesis
  • E. coli
  • Processing

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology

Cite this

Karamysheva, Z. N., Karamyshev, A. L., Ksenzenko, V. N., Shlyapnikov, M. G., Kayawa, A. V., & Nesmeyanova, M. A. (1997). Biogenesis and secretion of alkaline phosphatase and its mutant forms in Escherichia coli. IV. Changes in the signal peptide C-proximal domain affect processing. Molecular Biology, 31(5), 768-774.