SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal secretion signal

J Bacteriol. 2010 Nov;192(22):6093-8. doi: 10.1128/JB.00760-10. Epub 2010 Sep 10.

Abstract

Here we show that the type III secretion gatekeeper protein SepL resembles an aberrant effector protein in binding to a class 1 type III secretion chaperone (Orf12, here renamed CesL). We also show that short N-terminal fragments (≤70 amino acids) from SepL are capable of targeting fusion proteins for secretion and translocation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / genetics
  • Escherichia coli Proteins / metabolism*
  • Molecular Chaperones / metabolism*
  • Molecular Sequence Data
  • Protein Binding
  • Protein Sorting Signals
  • Protein Transport
  • Sequence Alignment
  • Sequence Homology, Amino Acid

Substances

  • Escherichia coli Proteins
  • Molecular Chaperones
  • Protein Sorting Signals
  • SepL protein, E coli