SepL Resembles an Aberrant Effector in Binding to a Class 1 Type III Secretion Chaperone and Carrying an N-Terminal Secretion Signal

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 f...

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Hlavní autoři: Younis, Rasha, Bingle, Lewis E. H., Rollauer, Sarah, Munera, Diana, Busby, Stephen J., Johnson, Steven, Deane, Janet E., Lea, Susan M., Frankel, Gad, Pallen, Mark J.
Médium: Artigo
Jazyk:Inglês
Vydáno: American Society for Microbiology (ASM) 2010
Témata:
Molecular Biology of Pathogens
On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC2976445/
https://ncbi.nlm.nih.gov/pubmed/20833800
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1128/JB.00760-10
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