Targeting efficiencies of various permutations of the consensus C-terminal tripeptide peroxisomal targeting signal

Bart W. Swinkels, Stephen J. Gould, Suresh Subramani

Research output: Contribution to journalArticle

Abstract

Two types of peptide signals are known to independently target proteins into the peroxisomal matrix. One of these is a consensus C-terminal tripeptide which is conserved in many microbody proteins derived from diverse species. The second signal is an N-terminal sequence found in a small subset of peroxisomal proteins. We have tested 18 possible variants of the consensus tripeptide targeting signal for their ability to facilitate the transport of a cytosolic passenger protein, chloramphenicol acetyltransferase, into peroxisomes of monkey kidney cells. Our results reveal the presence of a hierarchy of preferred amino acid substitutions at each position of the tripeptide.

Original languageEnglish (US)
Pages (from-to)133-136
Number of pages4
JournalFEBS Letters
Volume305
Issue number2
DOIs
StatePublished - Jun 29 1992
Externally publishedYes

Keywords

  • Peroxisomal targeting signal
  • Peroxisome biogenesis
  • Protein sorting
  • Protein trafficking
  • Topogenesis of peroxisomal protein

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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