TraG-like proteins of DNA transfer systems and of the Helicobacter pylori type IV secretion system:: Inner membrane gate for exported substrates?

被引:129
作者
Schröder, G
Krause, S
Zechner, EL
Traxler, B
Yeo, HJ
Lurz, R
Waksman, G
Lanka, E
机构
[1] Max Planck Inst Mol Genet, Abt Lehrach, D-14195 Berlin, Germany
[2] Washington Univ, Sch Med, Dept Biochem & Mol Biophys, St Louis, MO 63110 USA
[3] Univ Washington, Dept Genet, Seattle, WA 98195 USA
[4] Karl Franzens Univ Graz, Inst Mol Biol Biochem & Mikrobiol, A-8010 Graz, Austria
关键词
D O I
10.1128/JB.184.10.2767-2779.2002
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
TraG-like proteins are potential NTP hydrolases (NTPases) that are essential for DNA transfer in bacterial conjugation. They are thought to mediate interactions between the DNA-processing (Dtr) and the mating pair formation (Mpf) systems. TraG-like proteins also function as essential components of type W secretion systems of several bacterial pathogens such as Helicobacter pylori. Here we present the biochemical characterization of three members of the family of TraG-like proteins, TraG (RP4), TraD (F), and HP0524 (H. pylori). These proteins were found to have a pronounced tendency to form oligomers and were shown to bind DNA without sequence specificity. Standard NTPase assays indicated that these TraG-like proteins do not possess postulated NTP-hydrolyzing activity. Surface plasmon resonance was used to demonstrate an interaction between TraG and relaxase TraI of RP4. Topology analysis of TraG revealed that TraG is a transmembrane protein with cytosolic N and C termini and a short periplasmic domain close to the N terminus. We predict that multimeric inner membrane protein TraG forms a pore. A model suggesting that the relaxosome binds to the TraG pore via TraG-DNA and TraG-TraI interactions is presented.
引用
收藏
页码:2767 / 2779
页数:13
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