ArticleJournal of bacteriology2010
Biochemical dissection of the ATPase TraB, the VirB4 homologue of the Escherichia coli pKM101 conjugation machinery.
Article in Journal of bacteriology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed.
- Type IV secretion systems: reconciling diversity through a unified nomenclature.FEMS microbiology reviews · 2026Review
- Comparative Analysis of T4SS Molecular Architectures.Journal of microbiology and biotechnology · 2023Review
- Characterization of ConE, the VirB4 Homolog of the Integrative and Conjugative Element ICEJournal of bacteriology · 2023Article
- Oligomerization and Adjuvant Activity of Peptides Derived from the VirB4-like ATPase ofBiomolecules · 2023Article
- VirB4- and VirD4-Like ATPases, Components of a Putative Type 4C Secretion System in Clostridioides difficile.Journal of bacteriology · 2021Article
- Bacteria-Killing Type IV Secretion Systems.Frontiers in microbiology · 2019Review
- A unique cytoplasmic ATPase complex defines the Legionella pneumophila type IV secretion channel.Nature microbiology · 2018Article
- Agrobacterium-mediated plant transformation: biology and applications.The arabidopsis book · 2017Article
- The Mosaic Type IV Secretion Systems.EcoSal Plus · 2016Review
- Structure-Based Mutagenesis of Sulfolobus Turreted Icosahedral Virus B204 Reveals Essential Residues in the Virion-Associated DNA-Packaging ATPase.Journal of virology · 2015Article
- Article
- Mechanism and structure of the bacterial type IV secretion systems.Biochimica et biophysica acta · 2014Review
- Common requirement for the relaxosome of plasmid R1 in multiple activities of the conjugative type IV secretion system.Journal of bacteriology · 2014Article
- Structure of a type IV secretion system.Nature · 2014Article
- The hexameric structure of a conjugative VirB4 protein ATPase provides new insights for a functional and phylogenetic relationship with DNA translocases.The Journal of biological chemistry · 2012Article
- Enterococcus faecalis PrgJ, a VirB4-like ATPase, mediates pCF10 conjugative transfer through substrate binding.Journal of bacteriology · 2012Article
- Structure of the VirB4 ATPase, alone and bound to the core complex of a type IV secretion system.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Assembly and mechanisms of bacterial type IV secretion machines.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- Bacterial Type IV secretion systems: versatile virulence machines.Future microbiology · 2012Review
- Autoinhibitory regulation of TrwK, an essential VirB4 ATPase in type IV secretion systems.The Journal of biological chemistry · 2011Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Type IV secretion (T4S) systems are involved in several secretion processes, including secretion of virulence factors, such as toxins or transforming molecules, or bacterial conjugation whereby two mating bacteria exchange genetic material. T4S systems are generally composed of 12 protein components, three of which, termed VirB4, VirB11, and VirD4, are ATPases. VirB4 is the largest protein of the T4S system, is known to play a central role, and interacts with many other T4S system proteins. In this study, we have biochemically characterized the protein TraB, a VirB4 homologue from the pKM101 conjugation T4S system. We demonstrated that TraB is a modular protein, composed of two domains, both able to bind DNA in a non-sequence-specific manner. Surprisingly, both TraB N- and C-terminal domains can bind ATP, revealing a new degenerated nucleotide-binding site in the TraB N-terminal domain. TraB purified from the membrane forms stable dimers and is unable to hydrolyze ATP while, when purified from the soluble fraction, TraB can form hexamers capable of hydrolyzing ATP. Remarkably, both the N- and C-terminal domains display ATP-hydrolyzing activity. These properties define a new class of VirB4 proteins.
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