Structure of the conjugation surface exclusion protein TraT

Conjugal transfer of plasmids between bacteria is a major route for the spread of antimicrobial resistance. Many conjugative plasmids encode exclusion systems that inhibit redundant conjugation. In incompatibility group F (IncF) plasmids surface exclusion is mediated by the outer membrane protein TraT. Here we report the cryoEM structure of the TraT exclusion protein complex from the canonical F plasmid of Escherichia coli. TraT is a hollow homodecamer shaped like a chef's hat. In contrast to most outer membrane proteins, TraT spans the outer membrane using transmembrane α-helices. We develop a microscopy-based conjugation assay to probe the effects of directed mutagenesis on TraT. Our analysis provides no support for the idea that TraT has specific interactions with partner proteins. Instead, we infer that TraT is most likely to function by physical interference with conjugation. This work provides structural insight into a natural inhibitor of microbial gene transfer.

Authors

Institutions

Publication Details

Journal
Communications Biology
Published
2025-11-26
DOI
https://doi.org/10.1038/s42003-025-09102-8
Primary Topic
Bacterial Genetics and Biotechnology
Type
article
Field-Weighted Citation Impact
0.00

Funders

Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

Structure of the conjugation surface exclusion protein TraT

Camilla A.K. Lundgren, Alfredas Bukys, Achillefs N. Kapanidis, Ben C. Berks et al.
Communications Biology
Bacterial Genetics and Biotechnology
article

Structure of the conjugation surface exclusion protein TraT

Camilla A.K. Lundgren, Alfredas Bukys, Achillefs N. Kapanidis, Ben C. Berks, N X Chen, Susan M. Lea, Justin C. Deme, Hafez El Sayyed
article en

Abstract

Conjugal transfer of plasmids between bacteria is a major route for the spread of antimicrobial resistance. Many conjugative plasmids encode exclusion systems that inhibit redundant conjugation. In incompatibility group F (IncF) plasmids surface exclusion is mediated by the outer membrane protein TraT. Here we report the cryoEM structure of the TraT exclusion protein complex from the canonical F plasmid of Escherichia coli. TraT is a hollow homodecamer shaped like a chef's hat. In contrast to most outer membrane proteins, TraT spans the outer membrane using transmembrane α-helices. We develop a microscopy-based conjugation assay to probe the effects of directed mutagenesis on TraT. Our analysis provides no support for the idea that TraT has specific interactions with partner proteins. Instead, we infer that TraT is most likely to function by physical interference with conjugation. This work provides structural insight into a natural inhibitor of microbial gene transfer.

Communications BiologyVol. 8(1)
St. Jude Children's Research Hospital (US), Oxford Research Group (GB), University of Oxford (GB), Frederick National Laboratory for Cancer Research (US), National Cancer Institute (US), Center for Cancer Research (US)
Directorate for Biological Sciences, Clarendon Fund
Openalex Percentile: Top 61%
Bacterial Genetics and Biotechnology
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Structure of the conjugation surface exclusion protein TraT — Camilla A.K. Lundgren, Alfredas Bukys, et al. · Communications Biology (2025) | TGRS Research Map | TGRS