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

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. 
DOI: 10.1128/JB.00760-10

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Cite this paper

@article{Younis2010SepLRA, title={SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal secretion signal.}, author={Rasha Younis and Lewis E. H. Bingle and Sarah E Rollauer and Diana Munera and Stephen Busby and Steven M. Johnson and Janet E Deane and Susan M Lea and Gad M Frankel and Mark J. Pallen}, journal={Journal of bacteriology}, year={2010}, volume={192 22}, pages={6093-8} }