Can the topological distribution of membrane spanning amino acid residues be responsible for the recognition of signal peptides by signal peptide peptidases?

Research output: Contribution to journalArticle

Abstract

Signal peptides are selectively recognized and degraded by membrane associated proteases called as signal peptide peptidases. The hydrolysis of the signal peptide occurs only after its cleavage from the precursor. The possible reasons for this selectivity have been investigated. The results indicate that in signal peptides, leucine residues are clustered to a large extent on the same side of the membrane spanning alpha helix as the polar residues, but are distinctly separated along the length of the axis. Such topological differences in the distribution of amino acids on the surface of the membrane spanning alpha helix may play a crucial role in selective degradation of signal peptides.

Original languageEnglish (US)
Pages (from-to)537-546
Number of pages10
JournalBioscience Reports
Volume10
Issue number6
DOIs
StatePublished - Dec 1990
Externally publishedYes

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Protein Sorting Signals
Membranes
Amino Acids
Leucine
Hydrolysis
Peptide Hydrolases
Degradation
signal peptide peptidase
alpha-Helical Protein Conformation

Keywords

  • signal peptide degradation
  • signal peptide peptidase
  • topology

ASJC Scopus subject areas

  • Cell Biology
  • Biochemistry, Genetics and Molecular Biology(all)

Cite this

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abstract = "Signal peptides are selectively recognized and degraded by membrane associated proteases called as signal peptide peptidases. The hydrolysis of the signal peptide occurs only after its cleavage from the precursor. The possible reasons for this selectivity have been investigated. The results indicate that in signal peptides, leucine residues are clustered to a large extent on the same side of the membrane spanning alpha helix as the polar residues, but are distinctly separated along the length of the axis. Such topological differences in the distribution of amino acids on the surface of the membrane spanning alpha helix may play a crucial role in selective degradation of signal peptides.",
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author = "Ujwal Shinde",
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AB - Signal peptides are selectively recognized and degraded by membrane associated proteases called as signal peptide peptidases. The hydrolysis of the signal peptide occurs only after its cleavage from the precursor. The possible reasons for this selectivity have been investigated. The results indicate that in signal peptides, leucine residues are clustered to a large extent on the same side of the membrane spanning alpha helix as the polar residues, but are distinctly separated along the length of the axis. Such topological differences in the distribution of amino acids on the surface of the membrane spanning alpha helix may play a crucial role in selective degradation of signal peptides.

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