Solution characterization of the dynamic conjugative entry exclusion protein TraG

Bragagnolo, Nicholas; Audette, Gerald F.

doi:10.1063/4.0000171

Title: Solution characterization of the dynamic conjugative entry exclusion protein TraG

Journal Article · Tue Nov 01 00:00:00 EDT 2022 · Structural Dynamics

DOI:https://doi.org/10.1063/4.0000171· OSTI ID:1906895

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Centre for Research on Biomolecular Interactions, Department of Chemistry, York University, Toronto, Ontario M3J 1P3, Canada

The R100 plasmid and the secretion system it encodes are representative of F-like conjugative type IV secretion systems for the transmission of mobile DNA elements in gram-negative bacteria, serving as a major contributor to the spread of antibiotic resistance in bacterial pathogens. The TraG protein of F-like systems consists of a membrane-bound N-terminal domain and a periplasmic C-terminal domain, denoted TraG*. TraG* is essential in preventing redundant DNA transfer through a process termed entry exclusion. In the donor cell, it interacts with TraN to facilitate mating pair stabilization; however, if a mating pore forms between bacteria with identical plasmids, TraG* interacts with its cognate TraS in the inner membrane of the recipient bacterium to prevent redundant donor–donor conjugation. Structural studies of TraG* from the R100 plasmid have revealed the presence of a dynamic region between the N- and C-terminal domains of TraG. Thermofluor, circular dichroism, collision-induced unfolding–mass spectrometry, and size exclusion chromatography linked to multiangle light scattering and small angle x-ray scattering experiments indicated an N-terminal truncation mutant displayed higher stability and less disordered content relative to full-length TraG*. The 45 N-terminal residues of TraG* are hypothesized to serve as part of a flexible linker between the two independently functioning domains.

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Sponsoring Organization:: USDOE

Grant/Contract Number:: AC02-06CH11357

OSTI ID:: 1906895

Journal Information:: Structural Dynamics, Journal Name: Structural Dynamics Vol. 9 Journal Issue: 6; ISSN 2329-7778

Publisher:: American Institute of PhysicsCopyright Statement

Country of Publication:: United States

Language:: English

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