ArticleThe Journal of biological chemistry2011
Structure and function of PilQ, a secretin of the DNA transporter from the thermophilic bacterium Thermus thermophilus HB27.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Respiratory processes of early-evolved hyperthermophiles in sulfidic and low-oxygen geothermal microbial communities.Nature communications · 2025Article
- Type IV pili ofEcoSal Plus · 2024Review
- Natural transformation in Gram-negative bacteria thriving in extreme environments: from genes and genomes to proteins, structures and regulation.Extremophiles : life under extreme conditions · 2021Review
- CryoEM structure of the type IVa pilus secretin required for natural competence in Vibrio cholerae.Nature communications · 2020Article
- Article
- The traffic ATPase PilF interacts with the inner membrane platform of the DNA translocator and type IV pili fromFEBS open bio · 2019Article
- Functional dissection of the three N-terminal general secretory pathway domains and the Walker motifs of the traffic ATPase PilF from Thermus thermophilus.Extremophiles : life under extreme conditions · 2018Article
- Pull in and Push Out: Mechanisms of Horizontal Gene Transfer in Bacteria.Frontiers in microbiology · 2018Article
- Article
- A comprehensive guide to pilus biogenesis in Gram-negative bacteria.Nature reviews. Microbiology · 2017Review
- Three-Dimensional Structure of the Ultraoligotrophic Marine Bacterium "Candidatus Pelagibacter ubique".Applied and environmental microbiology · 2017Article
- Complete genome sequence ofStandards in genomic sciences · 2017Article
- Complete Genome Analysis ofFrontiers in microbiology · 2017Article
- Article
- Type IV Pilus Alignment Subcomplex Proteins PilN and PilO Form Homo- and Heterodimers in Vivo.The Journal of biological chemistry · 2016Article
- Topology and Structure/Function Correlation of Ring- and Gate-forming Domains in the Dynamic Secretin Complex of Thermus thermophilus.The Journal of biological chemistry · 2016Article
- The Type IV Pilus Assembly ATPase PilB of Myxococcus xanthus Interacts with the Inner Membrane Platform Protein PilC and the Nucleotide-binding Protein PilM.The Journal of biological chemistry · 2016Article
- Characterization of Outer Membrane Proteome of Akkermansia muciniphila Reveals Sets of Novel Proteins Exposed to the Human Intestine.Frontiers in microbiology · 2016Article
- Novel Role for PilNO in Type IV Pilus Retraction Revealed by Alignment Subcomplex Mutations.Journal of bacteriology · 2015Article
- Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Secretins are a family of large bacterial outer membrane protein complexes mediating the transport of complex structures, such as type IV pili, DNA and filamentous phage, or various proteins, such as extracellular enzymes and pathogenicity determinants. PilQ of the thermophilic bacterium Thermus thermophilus HB27 is a member of the secretin family required for natural transformation. Here we report the isolation, structural, and functional analyses of a unique PilQ from T. thermophilus. Native PAGE, gel filtration chromatography, and electrophoretic mobility shift analyses indicated that PilQ forms a macromolecular homopolymeric complex that binds dsDNA. Electron microscopy showed that the PilQ complex is 15 nm wide and 34 nm long and consists of an extraordinary stable "cone" and "cup" structure and five ring structures with a large central channel. Moreover, the electron microscopic images together with secondary structure analyses combined with structural data of type II protein secretion system and type III protein secretion system secretins suggest that the individual rings are formed by conserved domains of alternating α-helices and β-sheets. The unprecedented length of the PilQ complex correlated well with the distance between the inner and outer membrane of T. thermophilus. Indeed, PilQ was found immunologically in both membranes, indicating that the PilQ complex spans the entire cell periphery of T. thermophilus. This is consistent with the hypothesis that PilQ accommodates a PilA4 comprising pseudopilus mediating DNA transport across the outer membrane and periplasmic space in a single-step process.
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