SepL resembles an aberrant effector in binding to a class 1 type-III secretion chaperone and carrying an N-terminal secretion signal.
Research output: Contribution to journal › Article
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.
|Journal||Journal of Bacteriology|
|Publication status||Published - 10 Sep 2010|