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

Research output: Contribution to journalArticle

Authors

  • S Rollauer
  • D Munera
  • S Johnson
  • JE Deane
  • SM Lea
  • G Frankel

Colleges, School and Institutes

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.

Details

Original languageEnglish
JournalJournal of Bacteriology
Publication statusPublished - 10 Sep 2010