Type IV pilus structure and bacterial pathogenicity

Craig, Lisa; Pique, Michael E.; Tainer, John A.

doi:10.1038/nrmicro885

Cited by 690 publications

(800 citation statements)

References 145 publications

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“…PrePulG presumably inserts into the IM according to the positive-inside rule (62), with the positively charged N-terminal region of its prepilin signal sequence and prepilin peptidase cleavage site facing the cytoplasm and the C-terminal globular domain in the periplasm. This orientation is consistent with the fact that fusion of alkaline phosphatase (45) and ␤-lactamase (39) to the C terminus of full-length or truncated PulG leads to enzymatically active, periplasmically oriented membrane proteins and with the presence in pseudopilin PulK (41) and type IV pilins (12) of an intramolecular disulfide bond whose formation is catalyzed by periplasmic DsbA. The prepilin signal sequence promotes export though the Sec translocon, anchors the protein in the inner membrane, and promotes subunit assembly into a pseudopilus or type IV pilus filament.…”

Section: Discussionsupporting

confidence: 80%

“…T2SS machineries share a common origin and architecture and functional properties with systems involved in type IV pilus assembly and retraction, DNA uptake, and natural competence (64). Central to these machineries is their ability to assemble and disassemble filaments that either remain periplasmic and function in protein secretion (pseudopili) or extend well beyond the cell surface and play a role in adhesion, surface motility, or microcolony or biofilm formation (type IV pili) (12). The pseudopili and the closely related class A type IV pili are composed of one major pilin subunit and several minor pilins.…”

mentioning

confidence: 99%

“…This N-terminal hydrophobic helix leads directly into a 30-residue-long amphipathic ␣-helical region that is less well conserved and is followed by a globular domain composed of four antiparallel beta-sheets (24). In addition, type IVA pilins have a highly variable loop between 2 disulfide-bonded cysteine residues at their C-terminal ends (12).…”

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confidence: 99%

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Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

et al. 2007

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The pseudopilin PulG is an essential component of the pullulanase-specific type II secretion system from Klebsiella oxytoca. PulG is the major subunit of a short, thin-filament pseudopilus, which presumably elongates and retracts in the periplasm, acting as a dynamic piston to promote pullulanase secretion. It has a signal sequence-like N-terminal segment that, according to studies with green and red fluorescent protein chimeras, anchors unassembled PulG in the inner membrane. We analyzed the early steps of PulG inner membrane targeting and insertion in Escherichia coli derivatives defective in different protein targeting and export factors. The ␤-galactosidase activity in strains producing a PulG-LacZ hybrid protein increased substantially when the dsbA, dsbB, or all sec genes tested except secB were compromised by mutations. To facilitate analysis of native PulG membrane insertion, a leader peptidase cleavage site was engineered downstream from the N-terminal transmembrane segment (PrePulG*). Unprocessed PrePulG* was detected in strains carrying mutations in secA, secY, secE, and secD genes, including some novel alleles of secY and secD. Furthermore, depletion of the Ffh component of the signal recognition particle (SRP) completely abolished PrePulG* processing, without affecting the Sec-dependent export of periplasmic MalE and RbsB proteins. Thus, PulG is cotranslationally targeted to the inner membrane Sec translocase by SRP.

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Section: Discussionsupporting

confidence: 80%

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confidence: 99%

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Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

et al. 2007

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“…All of the e-pilin sequences lack the C-terminal portion of the sequence found in longer, more typical, PilA proteins, which code for beta sheet structures that form a large globular head (Craig et al, 2004;Giltner et al, 2012). Analysis of the structure of the Geobacter sulfurreducens e-pilus suggested that the lack of this C-terminus sequence permits the pilin monomers to pack more tightly than the larger pilin monomers found in most bacteria, yielding a thinner pilus diameter and positioning amino acids in patterns that confer conductivity (Malvankar et al, 2015).…”

Section: Resultsmentioning

confidence: 99%

The electrically conductive pili of Geobacter species are a recently evolved feature for extracellular electron transfer

et al. 2016

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The electrically conductive pili (e-pili) of Geobactersulfurreducens have environmental and practical significance because they can facilitate electron transfer to insoluble Fe(III) oxides; to other microbial species; and through electrically conductive biofilms. E-pili conductivity has been attributed to the truncated PilA monomer, which permits tight packing of aromatic amino acids to form a conductive path along the length of e-pili. In order to better understand the evolution and distribution of e-pili in the microbial world, type IVa PilA proteins from various Gram-negative and Gram-positive bacteria were examined with a particular emphasis on Fe(III)-respiring bacteria. E-pilin genes are primarily restricted to a tight phylogenetic group in the order Desulfuromonadales. The downstream gene in all but one of the Desulfuromonadales that possess an e-pilin gene is a gene previously annotated as 'pilA-C' that has characteristics suggesting that it may encode an outermembrane protein. Other genes associated with pilin function are clustered with e-pilin and 'pilA-C' genes in the Desulfuromonadales. In contrast, in the few bacteria outside the Desulfuromonadales that contain e-pilin genes, the other genes required for pilin function may have been acquired through horizontal gene transfer. Of the 95 known Fe(III)-reducing micro-organisms for which genomes are available, 80 % lack e-pilin genes, suggesting that e-pili are just one of several mechanisms involved in extracellular electron transport. These studies provide insight into where and when e-pili are likely to contribute to extracellular electron transport processes that are biogeochemically important and involved in bioenergy conversions.

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“…This includes Neisseria meningitides, which is the major cause of meningitis worldwide. Neisseria pathogenesis is mediated through molecular machines, particularly the type IV pili system (Craig et al, 2004). Recently, structures elucidated through a combination of cryo-electron microscopy and crystallography studies have revealed how type IV pilus fibers function, using surface groves as receptor-like binding sites for adherence and host cell interactions (Craig et al, 2006).…”

Section: Ros and Pathogensmentioning

confidence: 99%

Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair

2007

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This review is focused on proteins with key roles in pathways controlling either reactive oxygen species or DNA damage responses, both of which are essential for preserving the nervous system. An imbalance of reactive oxygen species or inappropriate DNA damage response likely causes mutational or cytotoxic outcomes, which may lead to cancer and/or aging phenotypes. Moreover, individuals with hereditary disorders in proteins of these cellular pathways have significant neurological abnormalities. Mutations in a superoxide dismutase, which removes oxygen free radicals, may cause the neurodegenerative disease amyotrophic lateral sclerosis. Additionally, DNA repair disorders that affect the brain to varying extents include ataxia-telangiectasia-like disorder, Cockayne syndrome or Werner syndrome. Here, we highlight recent advances gained through structural biochemistry studies on enzymes linked to these disorders and other related enzymes acting within the same cellular pathways. We describe the current understanding of how these vital proteins coordinate chemical steps and integrate cellular signaling and response events. Significantly, these structural studies may provide a set of master keys to developing a unified understanding of the survival mechanisms utilized after insults by reactive oxygen species and genotoxic agents, and also provide a basis for developing an informed intervention in brain tumor and neurodegenerative disease progression.

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Type IV pilus structure and bacterial pathogenicity

Cited by 690 publications

References 145 publications

Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

Signal Recognition Particle-Dependent Inner Membrane Targeting of the PulG Pseudopilin Component of a Type II Secretion System

The electrically conductive pili of Geobacter species are a recently evolved feature for extracellular electron transfer

Developing master keys to brain pathology, cancer and aging from the structural biology of proteins controlling reactive oxygen species and DNA repair

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