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

Rasha Younis, Lewis E H Bingle, Sarah E. Rollauer, Diana Munera, Stephen JW Busby, Steven Johnson, Janet E Deane, Susan M. Lea, Gad Frankel, Mark J Pallen

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23 Citations (Scopus)

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.

Original languageEnglish
Pages (from-to)6093-6098
Number of pages6
JournalJournal of Bacteriology
Volume192
Issue number22
DOIs
Publication statusPublished - Nov 2010
Externally publishedYes

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