Molecular Dissection of the Interface between the Type VI Secretion TssM Cytoplasmic Domain and the TssG Baseplate Component
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- 作者：Laureen Logger ; Marie-Sté ; phanie Aschtgen1 ; Marie Gué ; rin1 ; Eric Cascales ; cascales@imm.cnrs.fr" class="auth_mail" title="E-mail the corresponding author ; Eric Durand ; edurand@imm.cnrs.fr" class="auth_mail" title="E-mail the corresponding author ; eric13durand@yahoo.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：T6SS ; type VI secretion system ; BP ; baseplate ; MC ; membrane complex ; IM ; inner membrane ; OM ; outer membrane ; EAEC ; enteroaggregative Escherichia coli ; TMH ; transmembrane helices ; NTPase ; nucleotide triphosphatase ; NTP ; nucleotide triphosphate ; DPY-30 ; Dumpy-30 ; MPB ; 3-(N-maleimidylpropionyl) biocytin ; WT ; wild-type ; SIM ; sci-1-inducing medium ; AHT ; anhydrotetracyclin ; PBS ; phosphate-buffered saline ; spGFP ; super folder Green Fluorescent Protein ; DMSO ; Dimé ; thylsulfoxyde ; GTP ; Guanosine tri
- 刊名：Journal of Molecular Biology
- 出版年：2016
- 出版时间：6 November 2016
- 年：2016
- 卷：428
- 期：22
- 页码：4424-4437
- 全文大小：1392 K
文摘
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The T6SS TssM protein is constituted of three transmembrane segments.
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Transmembrane helices 2 and 3 delimitate a 35-kDa cytoplasmic domain.
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The TssM cytoplasmic loop is subdivided into two domains with NTPase and DPY30 folds.
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The TssM NTPase domain is lacking the catalytic site but interacts with TssK.
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The TssM DPY30 domain mediates oligomerisation and interaction with TssG.