TraG-Like Proteins of DNA Transfer Systems and of the Helicobacter pylori Type 
IV Secretion System: Inner Membrane Gate for Exported Substrates?

Schröder, Gunnar; Krause, Sabine; Zechner, Ellen L.; Traxler, Beth; Yeo, Hye-Jeong; Lurz, Rudi; Waksman, Gabriel; Lanka, Erich

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

Journal Article

TraG-Like Proteins of DNA Transfer Systems and of the Helicobacter pylori Type IV Secretion System: Inner Membrane Gate for Exported Substrates?

MPS-Authors

Schröder, Gunnar
Max Planck Society;

Krause, Sabine
Max Planck Society;

Lurz, Rudi
Max Planck Society;

Lanka, Erich
Max Planck Society;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

Citation

Schröder, G., Krause, S., Zechner, E. L., Traxler, B., Yeo, H.-J., Lurz, R., et al. (2002). TraG-Like Proteins of DNA Transfer Systems and of the Helicobacter pylori Type IV Secretion System: Inner Membrane Gate for Exported Substrates? Journal of Bacteriology, 184(10), 2767-2779.

Cite as: https://hdl.handle.net/11858/00-001M-0000-0010-8C02-5

Abstract

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 IV 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.