SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal secretion signal.
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ABSTRACT:
SUBMITTER: Younis R
PROVIDER: S-EPMC2976445 | biostudies-literature | 2010 Nov
REPOSITORIES: biostudies-literature
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SepL resembles an aberrant effector in binding to a class 1 type III secretion chaperone and carrying an N-terminal secretion signal.
Younis Rasha R Bingle Lewis E H LE Rollauer Sarah S Munera Diana D Busby Stephen J SJ Johnson Steven S Deane Janet E JE Lea Susan M SM Frankel Gad G Pallen Mark J MJ
Journal of bacteriology 20100910 22
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. ...[more]
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