Structure-Function Analysis of the TssL Cytoplasmic Domain Reveals a New Interaction between the Type VI Secretion Baseplate and Membrane Complexes
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- 作者：Abdelrahim Zoued1 ; 4 ; Chloé ; J. Cassaro1 ; Eric Durand1 ; Badreddine Douzi2 ; 3 ; 5 ; Alexandre P. Españ ; a1 ; 6 ; Christian Cambillau2 ; 3 ; Laure Journet1 ; Eric Cascales1 ; cascales@imm.cnrs.fr" class="auth_mail" title="E-mail the corresponding author
- 关键词：T6SS ; type VI secretion system ; BC ; baseplate complex ; MC ; membrane complex ; TMH ; transmembrane helices ; EAEC ; enteroaggregative Escherichia coli ; TssLCyto ; cytoplasmic domain of TssL ; GI ; Genbank accession ; BACTH ; bacterial two-hybrid ; TssMCyto ; cytoplasmic domain of TssM ; SPR ; surface plasmon resonance ; GFP ; green fluorescent protein ; LB ; Lysogeny broth ; TRX ; thioredoxin
- 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：4413-4423
- 全文大小：1141 K
文摘
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Systematic interaction studies reveal contact between the T6SS TssL and TssE subunits.
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The cytoplasmic domain of TssL delimitates a cleft that interacts with TssM.
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Two loops with distinct conformations mediate interactions with TssE and TssK.
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TssL interactions with TssM, TssE, and TssK are required for function of the T6SS.