作者: Gunnar Schröder , Sabine Krause , Ellen L. Zechner , Beth Traxler , Hye-Jeong Yeo
DOI: 10.1128/JB.184.10.2767-2779.2002
关键词:
摘要: TraG-like proteins are potential NTP hydrolases (NTPases) that essential for DNA transfer in bacterial conjugation. They thought to mediate interactions between the DNA-processing (Dtr) and mating pair formation (Mpf) systems. also function as components of type IV secretion systems several pathogens such Helicobacter pylori. Here we present biochemical characterization three members family proteins, TraG (RP4), TraD (F), HP0524 (H. pylori). These were found have a pronounced tendency form oligomers shown bind without sequence specificity. Standard NTPase assays indicated these do not possess postulated NTP-hydrolyzing activity. Surface plasmon resonance was used demonstrate an interaction relaxase TraI RP4. Topology analysis revealed is transmembrane protein with cytosolic N C termini short periplasmic domain close terminus. We predict multimeric inner membrane forms pore. A model suggesting relaxosome binds pore via TraG-DNA TraG-TraI presented.