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VirB6 and VirB10 from the Brucella type IV secretion system interact via the N‐terminal periplasmic domain of VirB6
Author(s) -
Villamil Giraldo Ana Maria,
Mary Charline,
Sivanesan Durgajini,
Baron Christian
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.05.051
Subject(s) - periplasmic space , secretion , terminal (telecommunication) , domain (mathematical analysis) , brucella , chemistry , brucella abortus , microbiology and biotechnology , type vi secretion system , biochemistry , biology , computer science , brucellosis , virology , escherichia coli , mathematics , gene , virulence , mathematical analysis , telecommunications
Type IV secretion systems are multi‐protein complexes that transfer macromolecules across the cell envelope of bacteria. Identifying the sites of interaction between the twelve proteins (VirB1–VirB11 and VirD4) that form these complexes is key to understanding their assembly and function. We have here used phage display, bacterial two‐hybrid and fluorescence‐based interaction assays to identify an N‐terminal domain of the inner membrane protein VirB6 as a site of interaction with the envelope‐spanning VirB10 protein. Our results are consistent with the notion that VirB6 acts in concert with VirB10 as well as with VirB8 during secretion system assembly and function.