Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching

Yamaguchi, Shigeru; Fujita, Hideo; Ishihara, Akira; Aizawa, Shin‐Ichi; Macnab, Robert M.

doi:10.1128/jb.166.1.187-193.1986

Cited by 195 publications

(168 citation statements)

References 25 publications

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“…All three proteins are involved in flagellar assembly, switching, and rotation (13,14). Since FliG is the motor protein most involved in speed and torque generation (12, 14, 15), we examined the binding between H-NS and FliG in fluorescence anisotropy assays.…”

Section: Hns Mutations Cause High Speed Flagella Rotationmentioning

confidence: 99%

Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Donato

Kawula

1998

Journal of Biological Chemistry

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Section: Hns Mutations Cause High Speed Flagella Rotationmentioning

confidence: 99%

Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Donato

Kawula

1998

Journal of Biological Chemistry

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“…All strains were derived from the nonflagellated S. typhimurium strain SJW2941 (9). The invA (10), invC (11), and invJ (12) mutant alleles were introduced into this strain by P22HTint-mediated transduction.…”

Section: Methodsmentioning

confidence: 99%

Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system

Kubori

Sukhan

Aizawa

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

314

338

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Many bacterial pathogens of plants and animals have evolved a specialized protein-secretion system termed type III to deliver bacterial proteins into host cells. These proteins stimulate or interfere with host cellular functions for the pathogen's benefit. The Salmonella typhimurium pathogenicity island 1 encodes one of these systems that mediates this bacterium's ability to enter nonphagocytic cells. Several components of this type III secretion system are organized in a supramolecular structure termed the needle complex. This structure is made of discrete substructures including a base that spans both membranes and a needle-like projection that extends outward from the bacterial surface. We demonstrate here that the type III secretion export apparatus is required for the assembly of the needle substructure but is dispensable for the assembly of the base. We show that the length of the needle segment is determined by the type III secretion associated protein InvJ. We report that InvG, PrgH, and PrgK constitute the base and that PrgI is the main component of the needle of the type III secretion complex. PrgI homologs are present in type III secretion systems from bacteria pathogenic for animals but are absent from bacteria pathogenic for plants. We hypothesize that the needle component may establish the specificity of type III secretion systems in delivering proteins into either plant or animal cells.bacterial pathogenesis ͉ type III secretion ͉ organelle assembly

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“…These flagellar motors can rotate in both clockwise (CW) and counterclockwise (CCW) directions (viewed from the outside of the cell), and the swimming pattern of the bacteria is controlled by reversal of the motor rotation (14). In E. coli, the FliG, FliM, FliN, MotA, and MotB proteins are involved with torque generation (Fig.…”

mentioning

confidence: 99%

“…In E. coli, the FliG, FliM, FliN, MotA, and MotB proteins are involved with torque generation (Fig. 1A) (14,15). FliG, FliM, and FliN constitute the flagellar rotor and are also involved with the CW/CCW switching.…”

mentioning

confidence: 99%

Gate-controlled proton diffusion and protonation-induced ratchet motion in the stator of the bacterial flagellar motor

Nishihara

Kitao

2015

Proc. Natl. Acad. Sci. U.S.A.

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The proton permeation process of the stator complex MotA/B in the flagellar motor of Escherichia coli was investigated. The atomic model structure of the transmembrane part of MotA/B was constructed based on the previously published disulfide cross-linking and tryptophan scanning mutations. The dynamic permeation of hydronium/ sodium ions and water molecule through the channel formed in MotA/B was observed using a steered molecular dynamics simulation. During the simulation, Leu46 of MotB acts as the gate for hydronium ion permeation, which induced the formation of water wire that may mediate the proton transfer to Asp32 on MotB. Free energy profiles for permeation were calculated by umbrella sampling. The free energy barrier for H 3 O + permeation was consistent with the proton transfer rate deduced from the flagellar rotational speed and number of protons per rotation, which suggests that the gating is the rate-limiting step. Structure and dynamics of the MotA/B with nonprotonated and protonated Asp32, Val43Met, and Val43Leu mutants in MotB were investigated using molecular dynamics simulation. A narrowing of the channel was observed in the mutants, which is consistent with the size-dependent ion selectivity. In MotA/B with the nonprotonated Asp32, the A3 segment in MotA maintained a kink whereas the protonation induced a straighter shape. Assuming that the cytoplasmic domain not included in the atomic model moves as a rigid body, the protonation/deprotonation of Asp32 is inferred to induce a ratchet motion of the cytoplasmic domain, which may be correlated to the motion of the flagellar rotor.proton transfer | bacterial flagellar motor | channel gating | ratchet motion | molecular dynamics B acterial flagella are multifuel engines that convert ion motive force to molecular motor rotation. Escherichia coli has a few proton-driven flagellar motors with stators (protein MotA/B complex) in the inner membrane that act as proton channels (1-5). In addition, Vibrio alginolyticus has a polar flagellum powered by sodium ions (6). Bacillus alcalophilus has motors driven by rubidium (Rb + ), potassium (K + ), and sodium ions (Na + ) that can be converted to Na + -driven motors by a single mutation (7).The proton transfer mechanism in membrane proteins is associated with water wire and/or a hydrogen bond chain (HBC) (8, 9). The water wire comprises water molecules aligned in a protein channel, where protons are transferred by hopping along the wire. Protons are conducted through the hydrogen bonds formed by the polar amino acid residues and water molecules along the proton transfer pathway in the HBC. Protons can also be transferred by diffusion of hydronium ions (H 3 O + ). The diffusion distance in a hydrophilic environment is short in a liquid (the lifetime in water is ca. 1 ps) (10, 11), but it should be longer in a more hydrophobic environment. H 3 O + forms a hydrogen bond (H bond) with the nearest neighbor water molecules and the carbonyl groups, and proton hopping along the H bonds is faster than diffusion of Na ...

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Subdivision of flagellar genes of Salmonella typhimurium into regions responsible for assembly, rotation, and switching

Cited by 195 publications

References 25 publications

Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Enhanced Binding of Altered H-NS Protein to Flagellar Rotor Protein FliG Causes Increased Flagellar Rotational Speed and Hypermotility in Escherichia coli

Molecular characterization and assembly of the needle complex of the Salmonella typhimurium type III protein secretion system

Gate-controlled proton diffusion and protonation-induced ratchet motion in the stator of the bacterial flagellar motor

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