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 Bingle, S Rollauer, D Munera, Stephen Busby, S Johnson, JE Deane, SM Lea, G Frankel, Mark Pallen

Research output: Contribution to journalArticle

22 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
JournalJournal of Bacteriology
DOIs
Publication statusPublished - 10 Sept 2010

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