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Flagellar Motor (flagellar + motor)
Selected AbstractsChemotaxis in Vibrio choleraeFEMS MICROBIOLOGY LETTERS, Issue 1 2004Markus A. Boin Abstract The ability of motile bacteria to swim toward or away from specific environmental stimuli, such as nutrients, oxygen, or light provides cells with a survival advantage, especially under nutrient-limiting conditions. This behavior, called chemotaxis, is mediated by the bacteria changing direction by briefly reversing the direction of rotation of the flagellar motors. A sophisticated signal transduction system, consisting of signal transducer proteins, a histidine kinase, a response regulator, a coupling protein, and enzymes that mediate sensory adaptation, relates the input signal to the flagellar motor. Chemotaxis has been extensively studied in bacteria such as Escherichia coli and Salmonella enterica serovar Typhimurium, and depends on the activity of single copies of proteins in a linear pathway. However, growing evidence suggests that chemotaxis in other bacteria is more complex with many bacterial species having multiple paralogues of the various chemotaxis genes found in E. coli and, in most cases, the detailed functions of these potentially redundant genes have not been elucidated. Although the completed genome of Vibrio cholerae, the causative agent of cholera, predicted a multitude of genes with homology to known chemotaxis-related genes, little is known about their relative contribution to chemotaxis or other cellular functions. Furthermore, the role of chemotaxis during the environmental or infectious phases of this organism is not yet fully understood. This review will focus on the complex relationship between chemotaxis and virulence in V. cholerae. [source] Cloning, overexpression, purification, crystallization and preliminary X-ray analysis of CheY3, a response regulator that directly interacts with the flagellar `switch complex' in Vibrio choleraeACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 8 2010Susmita Khamrui Vibrio cholerae is the aetiological agent of the severe diarrhoeal disease cholera. This highly motile organism uses the processes of motility and chemotaxis to travel and colonize the intestinal epithelium. Chemotaxis in V. cholerae is far more complex than that in Escherichia coli or Salmonella typhimurium, with multiple paralogues of various chemotaxis genes. In contrast to the single copy of the chemotaxis response-regulator protein CheY in E. coli, V. cholerae contains four CheYs (CheY1,CheY4), of which CheY3 is primarily responsible for interacting with the flagellar motor protein FliM, which is one of the major constituents of the `switch complex' in the flagellar motor. This interaction is the key step that controls flagellar rotation in response to environmental stimuli. CheY3 has been cloned, overexpressed and purified by Ni,NTA affinity chromatography followed by gel filtration. Crystals of CheY3 were grown in space group R3, with a calculated Matthews coefficient of 2.33,Å3,Da,1 (47% solvent content) assuming the presence of one molecule per asymmetric unit. [source] Cloning, purification and preliminary X-ray analysis of the C-terminal domain of Helicobacter pylori MotBACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 4 2008Anna Roujeinikova The C-terminal domain of MotB (MotB-C) contains a putative peptidoglycan-binding motif and is believed to anchor the MotA/MotB stator unit of the bacterial flagellar motor to the cell wall. Crystals of Helicobacter pylori MotB-C (138 amino-acid residues) were obtained by the hanging-drop vapour-diffusion method using polyethylene glycol as a precipitant. These crystals belong to space group P21, with unit-cell parameters a = 50.8, b = 89.5, c = 66.3,Å, , = 112.5°. The crystals diffract X-rays to at least 1.6,Å resolution using a synchrotron-radiation source. Self-rotation function and Matthews coefficient calculations suggest that the asymmetric unit contains one tetramer with 222 point-group symmetry. The anomalous difference Patterson maps calculated for an ytterbium-derivative crystal using diffraction data at a wavelength of 1.38,Å showed significant peaks on the v = 1/2 Harker section, suggesting that ab initio phase information could be derived from the MAD data. [source] Chemotaxis in Vibrio choleraeFEMS MICROBIOLOGY LETTERS, Issue 1 2004Markus A. Boin Abstract The ability of motile bacteria to swim toward or away from specific environmental stimuli, such as nutrients, oxygen, or light provides cells with a survival advantage, especially under nutrient-limiting conditions. This behavior, called chemotaxis, is mediated by the bacteria changing direction by briefly reversing the direction of rotation of the flagellar motors. A sophisticated signal transduction system, consisting of signal transducer proteins, a histidine kinase, a response regulator, a coupling protein, and enzymes that mediate sensory adaptation, relates the input signal to the flagellar motor. Chemotaxis has been extensively studied in bacteria such as Escherichia coli and Salmonella enterica serovar Typhimurium, and depends on the activity of single copies of proteins in a linear pathway. However, growing evidence suggests that chemotaxis in other bacteria is more complex with many bacterial species having multiple paralogues of the various chemotaxis genes found in E. coli and, in most cases, the detailed functions of these potentially redundant genes have not been elucidated. Although the completed genome of Vibrio cholerae, the causative agent of cholera, predicted a multitude of genes with homology to known chemotaxis-related genes, little is known about their relative contribution to chemotaxis or other cellular functions. Furthermore, the role of chemotaxis during the environmental or infectious phases of this organism is not yet fully understood. This review will focus on the complex relationship between chemotaxis and virulence in V. cholerae. [source] The loose coupling mechanism in molecular machines of living cellsGENES TO CELLS, Issue 1 2000Fumio Oosawa Living cells have molecular machines for free energy conversion, for example, sliding machines in muscle and other cells, flagellar motors in bacteria, and various ion pumps in cell membranes. They are constructed from protein molecules and work in the nm (nanometer), pN (piconewton) and ms (millisecond) ranges, without inertia. In 1980s, a question was raised of whether the input,output or influx,efflux coupling in these molecular machines is tight or loose, and an idea of loose coupling was proposed. Recently, the long-distance multistep sliding of a single myosin head on an actin filament, coupled with the hydrolysis of one ATP molecule, was observed by Yanagida's group using highly developed techniques of optical microscopy and micromanipulation. This gave direct evidence for the loose coupling between the chemical reaction and the mechanical event in the sliding machine. In this review, I will briefly describe a historical overview of the input,output problem in the molecular machines of living cells. [source] Signal Transfer in Haloarchaeal Sensory Rhodopsin, Transducer Complexes,PHOTOCHEMISTRY & PHOTOBIOLOGY, Issue 4 2008Jun Sasaki Membrane-inserted complexes consisting of two photochemically reactive sensory rhodopsin (SR) subunits flanking a homodimer of a transducing protein subunit (Htr) are used by halophilic archaea for sensing light gradients to modulate their swimming behavior (phototaxis). The SR,Htr complexes extend into the cytoplasm where the Htr subunits bind a his-kinase that controls a phosphorylation system that regulates the flagellar motors. This review focuses on current progress primarily on the mechanism of signal relay within the SRII,HtrII complexes from Natronomonas pharaonis and Halobacterium salinarum. The recent elucidation of a photoactive site steric trigger crucial for signal relay, advances in understanding the role of proton transfer from the chromophore to the protein in SRII activation, and the localization of signal relay to the membrane-embedded portion of the SRII,HtrII interface, are beginning to produce a clear picture of the signal transfer process. The SR,Htr complexes offer unprecedented opportunities to resolve first examples of the chemistry of signal relay between membrane proteins at the atomic level, which would provide a major contribution to the general understanding of dynamic interactions between integral membrane proteins. [source] | ||||||||||