Genomes and Genes
Gene Symbol: flgB
Description: flagellar component of cell-proximal portion of basal-body rod
Alias: ECK1058, JW1060, flbA
Species: Escherichia coli str. K-12 substr. MG1655
- Yamaguchi S, Aizawa S, Kihara M, Isomura M, Jones C, Macnab R. Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium. J Bacteriol. 1986;168:1172-9 pubmed..This switch complex is probably mounted to the base of the flagellar basal body and, via binding of the CheY and CheZ proteins, receives sensory information and uses it to control flagellar operation. ..
- Chun S, Parkinson J. Bacterial motility: membrane topology of the Escherichia coli MotB protein. Science. 1988;239:276-8 pubmed..Protease treatment of MotB in spheroplasts confirmed this view. The simple transmembrane organization of MotB is difficult to reconcile with a role as a proton conductor. ..
- Blair D, Berg H. Mutations in the MotA protein of Escherichia coli reveal domains critical for proton conduction. J Mol Biol. 1991;221:1433-42 pubmed..The clustering of the mutations provides independent support for the suggestion that MotA is a transmembrane proton channel and places significant constraints on models for the molecular mechanism of ion conduction. ..
- Braun T, Blair D. Targeted disulfide cross-linking of the MotB protein of Escherichia coli: evidence for two H(+) channels in the stator Complex. Biochemistry. 2001;40:13051-9 pubmed..Positions near the middle of the segment were inaccessible to sulhydryl reagents. Positions within 6-8 residues of either end, which includes residues around Asp32, were accessible. ..
- Yakushi T, Yang J, Fukuoka H, Homma M, Blair D. Roles of charged residues of rotor and stator in flagellar rotation: comparative study using H+-driven and Na+-driven motors in Escherichia coli. J Bacteriol. 2006;188:1466-72 pubmed..coli motor using both rotor and stator components from V. alginolyticus remained sensitive to mutation. Motor function in V. alginolyticus may be enhanced by the proteins MotX and MotY. ..
- Macnab R. How bacteria assemble flagella. Annu Rev Microbiol. 2003;57:77-100 pubmed..Exported substrates diffuse down a narrow channel in the growing structure and assemble at the distal end, often with the help of a capping structure. ..
- Zhou J, Sharp L, Tang H, Lloyd S, Billings S, Braun T, et al. Function of protonatable residues in the flagellar motor of Escherichia coli: a critical role for Asp 32 of MotB. J Bacteriol. 1998;180:2729-35 pubmed..We propose that Asp 32 of MotB functions as a proton-binding site in the bacterial flagellar motor and that no other conserved, protonatable residues function in this capacity. ..
- Maki Yonekura S, Yonekura K, Namba K. Domain movements of HAP2 in the cap-filament complex formation and growth process of the bacterial flagellum. Proc Natl Acad Sci U S A. 2003;100:15528-33 pubmed
- Khan S, Dapice M, Reese T. Effects of mot gene expression on the structure of the flagellar motor. J Mol Biol. 1988;202:575-84 pubmed..The concomitant loss of the rings and motility is consistent with the ring particles having a central role in the flagellar motor. ..
- Braun T, Al Mawsawi L, Kojima S, Blair D. Arrangement of core membrane segments in the MotA/MotB proton-channel complex of Escherichia coli. Biochemistry. 2004;43:35-45 pubmed
- Katayama E, Shiraishi T, Oosawa K, Baba N, Aizawa S. Geometry of the flagellar motor in the cytoplasmic membrane of Salmonella typhimurium as determined by stereo-photogrammetry of quick-freeze deep-etch replica images. J Mol Biol. 1996;255:458-75 pubmed..Various dimensions of the MS ring complex and the C ring projecting from the membrane were determined by digital stereo-photogrammetry, and a three-dimensional model of the total basal structure is presented. ..
- Welch M, Oosawa K, Aizawa S, Eisenbach M. Phosphorylation-dependent binding of a signal molecule to the flagellar switch of bacteria. Proc Natl Acad Sci U S A. 1993;90:8787-91 pubmed..This study provides a biochemical demonstration of binding of a signal molecule to the bacterial switch and demonstrates directly that phosphorylation regulates the activity of this molecule. ..
- Sowa Y, Rowe A, Leake M, Yakushi T, Homma M, Ishijima A, et al. Direct observation of steps in rotation of the bacterial flagellar motor. Nature. 2005;437:916-9 pubmed..Backwards steps despite the absence of the flagellar switching protein CheY indicate a small change in free energy per step, similar to that of a single ion transit. ..
- Hasegawa K, Yamashita I, Namba K. Quasi- and nonequivalence in the structure of bacterial flagellar filament. Biophys J. 1998;74:569-75 pubmed
- Thomas D, Morgan D, DeRosier D. Rotational symmetry of the C ring and a mechanism for the flagellar rotary motor. Proc Natl Acad Sci U S A. 1999;96:10134-9 pubmed..Movement results from the swapping of stud-bound levers with M ring-bound levers. The model predicts that both the M and C rings rotate in the same direction but at different speeds. ..
- Saijo Hamano Y, Uchida N, Namba K, Oosawa K. In vitro characterization of FlgB, FlgC, FlgF, FlgG, and FliE, flagellar basal body proteins of Salmonella. J Mol Biol. 2004;339:423-35 pubmed..study the structure of the rod in detail, we have established purification procedures for Salmonella rod proteins, FlgB, FlgC, FlgF, FlgG, and also for FliE, a rod adapter protein, from an Escherichia coli expression system...
- Suzuki H, Yonekura K, Namba K. Structure of the rotor of the bacterial flagellar motor revealed by electron cryomicroscopy and single-particle image analysis. J Mol Biol. 2004;337:105-13 pubmed
- Jones C, Macnab R, Okino H, Aizawa S. Stoichiometric analysis of the flagellar hook-(basal-body) complex of Salmonella typhimurium. J Mol Biol. 1990;212:377-87 pubmed..The distal rod protein (FlgG) is present at approximately 26 subunits, while the proximal rod proteins (FlgB, FlgC and FlgF) are present at only approximately six subunits each...
- Samatey F, Imada K, Nagashima S, Vonderviszt F, Kumasaka T, Yamamoto M, et al. Structure of the bacterial flagellar protofilament and implications for a switch for supercoiling. Nature. 2001;410:331-7 pubmed..By simulated extension of the protofilament model, we have identified possible switch regions responsible for the bi-stable mechanical switch that generates the 0.8 A difference in repeat distance. ..
- Suzuki H, Yonekura K, Murata K, Hirai T, Oosawa K, Namba K. A structural feature in the central channel of the bacterial flagellar FliF ring complex is implicated in type III protein export. J Struct Biol. 1998;124:104-14 pubmed..This suggests that a domain of FliF partially occupies the central channel to be involved in the export and gate mechanism, and the domain changes its conformation depending on the ionic strength. ..
- Garza A, Bronstein P, Valdez P, Harris Haller L, Manson M. Extragenic suppression of motA missense mutations of Escherichia coli. J Bacteriol. 1996;178:6116-22 pubmed
- Ridgway H, Silverman M, Simon M. Localization of proteins controlling motility and chemotaxis in Escherichia coli. J Bacteriol. 1977;132:657-65 pubmed..Differences in the intracellular locations of the che and mot gene prodcuts presumably reflect the functional attributes of these components. ..
- Fahrner K, Block S, Krishnaswamy S, Parkinson J, Berg H. A mutant hook-associated protein (HAP3) facilitates torsionally induced transformations of the flagellar filament of Escherichia coli. J Mol Biol. 1994;238:173-86 pubmed..The N-terminal sequence of HAP3 was found to be similar to the N-terminal sequence of flagellin, and the possibility that it provides a nucleation site for the C-terminal region of flagellin is discussed. ..
- Jones C, Homma M, Macnab R. Identification of proteins of the outer (L and P) rings of the flagellar basal body of Escherichia coli. J Bacteriol. 1987;169:1489-92 pubmed..Gene-polypeptide correlations from other studies enabled us to complete gene-polypeptide-structure correspondences for these two proteins as flaM----39-kilodalton protein----P ring and flaY----26-kilodalton protein----L ring. ..
- Reid S, Leake M, Chandler J, Lo C, Armitage J, Berry R. The maximum number of torque-generating units in the flagellar motor of Escherichia coli is at least 11. Proc Natl Acad Sci U S A. 2006;103:8066-71 pubmed..Speed increments at high numbers of units are smaller than those at low numbers, indicating that not all units in a fully induced motor are equivalent. ..
- Garza A, Harris Haller L, Stoebner R, Manson M. Motility protein interactions in the bacterial flagellar motor. Proc Natl Acad Sci U S A. 1995;92:1970-4 pubmed..This finding suggests that the postulated Mot-protein complex may be in close proximity to FliG at the stator-rotor interface of the flagellar motor. ..
- Sosinsky G, Francis N, DeRosier D, Wall J, Simon M, Hainfeld J. Mass determination and estimation of subunit stoichiometry of the bacterial hook-basal body flagellar complex of Salmonella typhimurium by scanning transmission electron microscopy. Proc Natl Acad Sci U S A. 1992;89:4801-5 pubmed..the mass of the rod is consistent with a composition of approximately 6 copies each of three of the rod proteins FlgB, FlgC, and FlgF and approximately 26 copies of FlgG as determined by Jones et al. [Jones, C. J., Macnab, R. M...
- Kojima S, Blair D. Solubilization and purification of the MotA/MotB complex of Escherichia coli. Biochemistry. 2004;43:26-34 pubmed..35)S-radiolabeling showed that MotA and MotB are present in a 2:1 ratio in the complex. Purified MotA/MotB complexes should enable in vitro study of the proton-induced conformational change and other aspects of stator function. ..
- Grünenfelder B, Gehrig S, Jenal U. Role of the cytoplasmic C terminus of the FliF motor protein in flagellar assembly and rotation. J Bacteriol. 2003;185:1624-33 pubmed..These results provide genetic support for a model in which only a short stretch of amino acids at the immediate C terminus of FliF is required for flagellar assembly through stable interaction with the FliG switch protein. ..
- Maki S, Vonderviszt F, Furukawa Y, Imada K, Namba K. Plugging interactions of HAP2 pentamer into the distal end of flagellar filament revealed by electron microscopy. J Mol Biol. 1998;277:771-7 pubmed..This also allows us to model the axial domain arrangement of flagellin subunit in the filament. ..
- Minamino T, Yamaguchi S, Macnab R. Interaction between FliE and FlgB, a proximal rod component of the flagellar basal body of Salmonella. J Bacteriol. 2000;182:3029-36 pubmed..which caused extremely poor flagellation and swarming, generated extragenic suppressors, all of which mapped to flgB, one of four genes encoding the basal body rod; the fliE flgB pseudorevertants were better flagellated and swarmed ..
- Garza A, Biran R, Wohlschlegel J, Manson M. Mutations in motB suppressible by changes in stator or rotor components of the bacterial flagellar motor. J Mol Biol. 1996;258:270-85 pubmed..We suggest that most of the suppressors restore motility by introducing compensatory realignments in MotA or FliG. ..