ArticleMolecular microbiology2013
Structure of a translocation signal domain mediating conjugative transfer by type IV secretion systems.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- Type IV secretion systems: from structures to mechanisms.The EMBO journal · 2025Review
- Cryo-EM Structure of the relaxosome, a complex essential for bacterial mating and the spread of antibiotic resistance genes.Nature communications · 2025Article
- The F plasmid conjutome: the repertoire ofmSphere · 2024Article
- Translocation of YopJ family effector proteins through the VirB/VirD4 T4SS ofProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Chimeric systems composed of swapped Tra subunits between distantly-related F plasmids reveal striking plasticity among type IV secretion machines.PLoS genetics · 2024Article
- Chimeric systems composed of swapped Tra subunits between distantly-related F plasmids reveal striking plasticity among type IV secretion machines.bioRxiv : the preprint server for biology · 2023Article
- DNA Transport through the Dynamic Type IV Secretion System.Infection and immunity · 2023Review
- Structural basis for effector recognition by an antibacterial type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Article
- Type IV secretion systems: Advances in structure, function, and activation.Molecular microbiology · 2021Review
- Secrete or perish: The role of secretion systems inComputational and structural biotechnology journal · 2021Review
- The Impact ofFrontiers in microbiology · 2021Review
- The TraK accessory factor activates substrate transfer through the pKM101 type IV secretion system independently of its role in relaxosome assembly.Molecular microbiology · 2020Article
- The Rich Tapestry of Bacterial Protein Translocation Systems.The protein journal · 2019Review
- Biological and Structural Diversity of Type IV Secretion Systems.Microbiology spectrum · 2019Review
- From conjugation to T4S systems in Gram-negative bacteria: a mechanistic biology perspective.EMBO reports · 2019Review
- Versatility of the BID Domain: Conserved Function as Type-IV-Secretion-Signal and Secondarily Evolved Effector Functions WithinFrontiers in microbiology · 2019Review
- Type IV secretion in Gram-negative and Gram-positive bacteria.Molecular microbiology · 2018Review
- Article
- The BID Domain of Type IV Secretion Substrates Forms a Conserved Four-Helix Bundle Topped with a Hook.Structure (London, England : 1993) · 2017Article
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8 authors.
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Abstract
Relaxases are proteins responsible for the transfer of plasmid and chromosomal DNA from one bacterium to another during conjugation. They covalently react with a specific phosphodiester bond within DNA origin of transfer sequences, forming a nucleo-protein complex which is subsequently recruited for transport by a plasmid-encoded type IV secretion system. In previous work we identified the targeting translocation signals presented by the conjugative relaxase TraI of plasmid R1. Here we report the structure of TraI translocation signal TSA. In contrast to known translocation signals we show that TSA is an independent folding unit and thus forms a bona fide structural domain. This domain can be further divided into three subdomains with striking structural homology with helicase subdomains of the SF1B family. We also show that TSA is part of a larger vestigial helicase domain which has lost its helicase activity but not its single-stranded DNA binding capability. Finally, we further delineate the binding site responsible for translocation activity of TSA by targeting single residues for mutations. Overall, this study provides the first evidence that translocation signals can be part of larger structural scaffolds, overlapping with translocation-independent activities.
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