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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書目詳細資料
Main Authors: Younis, R, Bingle, L, Rollauer, S, Munera, D, Busby, S, Johnson, S, Deane, J, Lea, S, Frankel, G, Pallen, M
格式: Journal article
語言:English
出版: 2010
實物特徵
總結: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.