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

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

Author information

1
School of Biosciences, University of Birmingham, Edgbaston, Birmingham, United Kingdom.

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.

PMID:
20833800
PMCID:
PMC2976445
DOI:
10.1128/JB.00760-10
[Indexed for MEDLINE]
Free PMC Article

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