Literature DB >> 3537316

Pairwise perturbation of flagellin subunits. The structural basis for the differences between plain and complex bacterial flagellar filaments.

S Trachtenberg, D J DeRosier, S Aizawa, R M Macnab.   

Abstract

Although plain and complex bacterial flagellar filaments differ in their physical properties and helical symmetry, they both appear to derive from a common underlying structure. Analysis of electron micrographs of complex filaments of Rhizobium lupini revealed that the unit cell has twice the length of that of plain filaments, with a corresponding reduction in helical symmetry whereby the six-start helical family present in plain filaments collapses into a three-start family. Mass per unit length measurements were made by scanning transmission electron microscopy. These, together with the unit cell dimensions and the molecular weight of the flagellin monomer, enabled the number of monomers per unit cell to be estimated. Whereas plain filaments have a single monomer per unit cell, complex filaments have two. These results suggest that complex filament structure differs from plain filament structure by a pairwise perturbation, or interaction, of the flagellin monomers. The additional bonding interactions involved in the perturbation in the complex filament may make it more rigid than the plain filament, which has no such perturbation.

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Year:  1986        PMID: 3537316     DOI: 10.1016/0022-2836(86)90242-1

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  18 in total

1.  A three-start helical sheath on the flagellar filament of Caulobacter crescentus.

Authors:  S Trachtenberg; D J DeRosier
Journal:  J Bacteriol       Date:  1992-10       Impact factor: 3.490

2.  Mutations in the two flagellin genes of Rhizobium meliloti.

Authors:  K Bergman; E Nulty; L H Su
Journal:  J Bacteriol       Date:  1991-06       Impact factor: 3.490

3.  Expression of two Rhizobium meliloti flagellin genes and their contribution to the complex filament structure.

Authors:  E Pleier; R Schmitt
Journal:  J Bacteriol       Date:  1991-03       Impact factor: 3.490

4.  Bacterial flagellar microhydrodynamics: Laminar flow over complex flagellar filaments, analog archimedean screws and cylinders, and its perturbations.

Authors:  Shlomo Trachtenberg; Dalia Fishelov; Matania Ben-Artzi
Journal:  Biophys J       Date:  2003-09       Impact factor: 4.033

5.  Role of divalent cations in the subunit associations of complex flagella from Rhizobium meliloti.

Authors:  J B Robinson; O H Tuovinen; W D Bauer
Journal:  J Bacteriol       Date:  1992-06       Impact factor: 3.490

6.  Antigenic relatedness and N-terminal sequence homology define two classes of periplasmic flagellar proteins of Treponema pallidum subsp. pallidum and Treponema phagedenis.

Authors:  S J Norris; N W Charon; R G Cook; M D Fuentes; R J Limberger
Journal:  J Bacteriol       Date:  1988-09       Impact factor: 3.490

7.  Real-time imaging of fluorescent flagellar filaments of Rhizobium lupini H13-3: flagellar rotation and pH-induced polymorphic transitions.

Authors:  Birgit Scharf
Journal:  J Bacteriol       Date:  2002-11       Impact factor: 3.490

8.  Mutational analysis of the Rhizobium lupini H13-3 and Sinorhizobium meliloti flagellin genes: importance of flagellin A for flagellar filament structure and transcriptional regulation.

Authors:  B Scharf; H Schuster-Wolff-Bühring; R Rachel; R Schmitt
Journal:  J Bacteriol       Date:  2001-09       Impact factor: 3.490

9.  Rhizobium meliloti swims by unidirectional, intermittent rotation of right-handed flagellar helices.

Authors:  R Götz; R Schmitt
Journal:  J Bacteriol       Date:  1987-07       Impact factor: 3.490

10.  Identification and sequence analysis of two related flagellin genes in Rhizobium meliloti.

Authors:  E Pleier; R Schmitt
Journal:  J Bacteriol       Date:  1989-03       Impact factor: 3.490

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