Literature DB >> 7402342

Formation of helical filaments by copolymerization of two types of 'straight' flagellins.

R Kamiya, S Asakura, S Yamaguchi.   

Abstract

Bacterial flagella undergo transition between several discrete types of left-handed and right-handed helical structures when exposed to acidic or alkaline pH, or to mechanical force. Calladine and ourselves have presented models to explain such polymorphism, assuming that protein subunits (flagellin) in a flagellum can be transformed into two conformations (L- and R-states) depending on the species of flagellin and on the environmental conditions. An obvious prediction from these 'two-state' models is that there should be two types of straight flagella (L- and R-types) that are made up exclusively of flagellins in either the L-state or the R-state. We have shown that straight flagella from two species of mutants, Salmonella SJ814 (ref. 6) and Escherichia coli hag 177 (ref. 7), are closely similar to the predicted R- and L-types, respectively. Recently we have isolated 10 strains of straight-flagellar mutants of Salmonella. We show here that their flagella can also be classified into the L- and R-types, and that copolymerization of flagellins from two heterologous types (L and R) makes discrete types of helical filaments, whereas that of homologous pairs of flagellins (L and L, or R and R) makes only straight filaments.

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Year:  1980        PMID: 7402342     DOI: 10.1038/286628a0

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


  15 in total

1.  Force-extension measurements on bacterial flagella: triggering polymorphic transformations.

Authors:  Nicholas C Darnton; Howard C Berg
Journal:  Biophys J       Date:  2006-12-15       Impact factor: 4.033

2.  Microtubules soften due to cross-sectional flattening.

Authors:  Edvin Memet; Feodor Hilitski; Margaret A Morris; Walter J Schwenger; Zvonimir Dogic; L Mahadevan
Journal:  Elife       Date:  2018-06-01       Impact factor: 8.140

3.  A theoretical model of Aquifex pyrophilus flagellin: implications for its thermostability.

Authors:  V Raghu Ram Malapaka; Brian C Tripp
Journal:  J Mol Model       Date:  2006-01-13       Impact factor: 1.810

4.  Conformational change of flagellin for polymorphic supercoiling of the flagellar filament.

Authors:  Saori Maki-Yonekura; Koji Yonekura; Keiichi Namba
Journal:  Nat Struct Mol Biol       Date:  2010-03-14       Impact factor: 15.369

5.  Quasi- and nonequivalence in the structure of bacterial flagellar filament.

Authors:  K Hasegawa; I Yamashita; K Namba
Journal:  Biophys J       Date:  1998-01       Impact factor: 4.033

6.  Direct interaction of flagellin termini essential for polymorphic ability of flagellar filament.

Authors:  Y Mimori-Kiyosue; F Vonderviszt; I Yamashita; Y Fujiyoshi; K Namba
Journal:  Proc Natl Acad Sci U S A       Date:  1996-12-24       Impact factor: 11.205

7.  Archaeal flagellin combines a bacterial type IV pilin domain with an Ig-like domain.

Authors:  Tatjana Braun; Matthijn R Vos; Nir Kalisman; Nicholas E Sherman; Reinhard Rachel; Reinhard Wirth; Gunnar F Schröder; Edward H Egelman
Journal:  Proc Natl Acad Sci U S A       Date:  2016-08-30       Impact factor: 11.205

8.  Locations of hook-associated proteins in flagellar structures of Salmonella typhimurium.

Authors:  M Homma; T Iino
Journal:  J Bacteriol       Date:  1985-04       Impact factor: 3.490

9.  The flagellar filament of Rhodobacter sphaeroides: pH-induced polymorphic transitions and analysis of the fliC gene.

Authors:  D S Shah; T Perehinec; S M Stevens; S I Aizawa; R E Sockett
Journal:  J Bacteriol       Date:  2000-09       Impact factor: 3.490

10.  Key amino acid residues involved in the transitions of L- to R-type protofilaments of the Salmonella flagellar filament.

Authors:  Fumio Hayashi; Hidetoshi Tomaru; Eiji Furukawa; Kanae Ikeda; Hiroko Fukano; Kenji Oosawa
Journal:  J Bacteriol       Date:  2013-05-31       Impact factor: 3.490

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