2007
DOI: 10.1099/mic.0.2006/001297-0
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Interaction between the co-inherited TraG coupling protein and the TraJ membrane-associated protein of the H-plasmid conjugative DNA transfer system resembles chromosomal DNA translocases

Abstract: Bacterial conjugation is a DNA transfer event that requires three plasmid-encoded multi-protein complexes: the membrane-spanning mating pair formation (Mpf) complex, the cytoplasmic nucleoprotein relaxosome complex, and a homo-multimeric coupling protein that links the Mpf and relaxosome at the cytoplasmic membrane. Bacterial two-hybrid (BTH) technology and immunoprecipitation were used to demonstrate an interaction between the IncH plasmid-encoded transfer protein TraJ and the coupling protein TraG. TraJ is e… Show more

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Cited by 17 publications
(21 citation statements)
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“…TraG R27 -like proteins (but not TraG RP4 , TraD F , or TrwB R388 ) bind TraJ R27 in vitro. The close juxtaposition of genes for TraJ and TraG, the multimembrane-spanning character of TraJ proteins, and a sequence identity of 21.4% between TraJ R27 and the N terminus of the FtsK translocase support a proposal that TraJ and TraG cumulatively represent the domain architecture of the larger FtsK/SpoIIIE DNA translocases (118).…”
Section: T4cp Heterogeneitymentioning
confidence: 54%
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“…TraG R27 -like proteins (but not TraG RP4 , TraD F , or TrwB R388 ) bind TraJ R27 in vitro. The close juxtaposition of genes for TraJ and TraG, the multimembrane-spanning character of TraJ proteins, and a sequence identity of 21.4% between TraJ R27 and the N terminus of the FtsK translocase support a proposal that TraJ and TraG cumulatively represent the domain architecture of the larger FtsK/SpoIIIE DNA translocases (118).…”
Section: T4cp Heterogeneitymentioning
confidence: 54%
“…2 and 3) (118). These T4CPs resemble TraG RP4 , TrwBR 388 , and VirD4 At in overall size and predicted N-terminal TM domains, but they typically possess much smaller (ϳ4 residues) periplasmic domains.…”
Section: T4cp Heterogeneitymentioning
confidence: 96%
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“…We show that interactions between TraD and other F-encoded factors (probably proteins) facilitate the assembly of a large and possibly heteromeric complex. The participation of other proteins in in vivo assembly is not surprising, given the role of CPs as a link between substrate processing and secretion modules; CPs have been shown to interact with several cytoplasmic and extracellular T4SS components in both conjugative (5,11,12,14,18,19,21,35,36,46,49) and virulence (3,4,11,37) models.…”
Section: Discussionmentioning
confidence: 99%
“…TraJ subunits are hydrophobic, multi-pass membrane proteins with sequence relatedness to the N terminus of FtsK translocase. Thus, it was proposed that TraJ and TraG cumulatively represent the domain architecture of the larger FtsK/SpoIIIE DNA translocases [91]. Members of another T4CP subfamily, represented by S. agalactiae pIP501 and B. cenecapacia AU1054, appear to lack N-terminal TM domains entirely, but upstream of the genes for these T4CPs are genes coding for small proteins (~150–200 residues) with 2 – 4 predicted TM domains.…”
Section: The T4cp Substrate Receptormentioning
confidence: 99%