Literature DB >> 3313394

Identification of the M-ring protein of the flagellar motor of Salmonella typhimurium.

M Homma1, S Aizawa, G E Dean, R M Macnab.   

Abstract

The M ring is a substructure of the flagellar basal body of bacteria, which lies in the cytoplasmic membrane and is therefore close to the site where the energy of the transmembrane proton potential is converted into mechanical work of rotation of the motor. The protein from which this ring is constructed has not been identified. Flagellar hook-basal body complexes from Salmonella typhimurium were used as the immunogen for the preparation of monoclonal antibodies. An antibody obtained was directed against a major basal-body component, a 65-kDa protein that from mutant studies has been assigned as the product of the flaAII.1 gene. By immunoelectron microscopy, the antibody was observed to bind the innermost feature of the basal body: the cytoplasmic-facing surface of the M ring. We conclude that the 65-kDa protein is a component--probably the main component--of this important substructure of the flagellar motor.

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Year:  1987        PMID: 3313394      PMCID: PMC299320          DOI: 10.1073/pnas.84.21.7483

Source DB:  PubMed          Journal:  Proc Natl Acad Sci U S A        ISSN: 0027-8424            Impact factor:   11.205


  33 in total

1.  Identification of a bacterial sensing protein and effects of its elevated expression.

Authors:  D O Clegg; D E Koshland
Journal:  J Bacteriol       Date:  1985-04       Impact factor: 3.490

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

Authors:  S Yamaguchi; H Fujita; A Ishihara; S Aizawa; R M Macnab
Journal:  J Bacteriol       Date:  1986-04       Impact factor: 3.490

3.  Nucleotide sequence of the Escherichia coli motB gene and site-limited incorporation of its product into the cytoplasmic membrane.

Authors:  J Stader; P Matsumura; D Vacante; G E Dean; R M Macnab
Journal:  J Bacteriol       Date:  1986-04       Impact factor: 3.490

4.  Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimurium.

Authors:  S Yamaguchi; S Aizawa; M Kihara; M Isomura; C J Jones; R M Macnab
Journal:  J Bacteriol       Date:  1986-12       Impact factor: 3.490

5.  The flaFIX gene product of Salmonella typhimurium is a flagellar basal body component with a signal peptide for export.

Authors:  M Homma; Y Komeda; T Iino; R M Macnab
Journal:  J Bacteriol       Date:  1987-04       Impact factor: 3.490

6.  Identification of proteins of the outer (L and P) rings of the flagellar basal body of Escherichia coli.

Authors:  C J Jones; M Homma; R M Macnab
Journal:  J Bacteriol       Date:  1987-04       Impact factor: 3.490

7.  Localization and stoichiometry of hook-associated proteins within Salmonella typhimurium flagella.

Authors:  T Ikeda; M Homma; T Iino; S Asakura; R Kamiya
Journal:  J Bacteriol       Date:  1987-03       Impact factor: 3.490

8.  Excretion of unassembled hook-associated proteins by Salmonella typhimurium.

Authors:  M Homma; T Iino
Journal:  J Bacteriol       Date:  1985-12       Impact factor: 3.490

9.  Attachment of flagellar basal bodies to the cell envelope: specific attachment to the outer, lipopolysaccharide membrane and the cyoplasmic membrane.

Authors:  M L DePamphilis; J Adler
Journal:  J Bacteriol       Date:  1971-01       Impact factor: 3.490

10.  Structural genes for flagellar hook-associated proteins in Salmonella typhimurium.

Authors:  M Homma; K Kutsukake; T Iino
Journal:  J Bacteriol       Date:  1985-08       Impact factor: 3.490

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  25 in total

1.  Deletion analysis of the flagellar switch protein FliG of Salmonella.

Authors:  M Kihara; G U Miller; R M Macnab
Journal:  J Bacteriol       Date:  2000-06       Impact factor: 3.490

2.  Effects of lipoprotein biogenesis mutations on flagellar assembly in Salmonella.

Authors:  Frank E Dailey; Robert M Macnab
Journal:  J Bacteriol       Date:  2002-02       Impact factor: 3.490

3.  Role of the cytoplasmic C terminus of the FliF motor protein in flagellar assembly and rotation.

Authors:  Björn Grünenfelder; Stefanie Gehrig; Urs Jenal
Journal:  J Bacteriol       Date:  2003-03       Impact factor: 3.490

4.  Location of the basal disk and a ringlike cytoplasmic structure, two additional structures of the flagellar apparatus of Wolinella succinogenes.

Authors:  S C Schuster; E Baeuerlein
Journal:  J Bacteriol       Date:  1992-01       Impact factor: 3.490

5.  The flagellar basal body-associated protein FlgT is essential for a novel ring structure in the sodium-driven Vibrio motor.

Authors:  Hiroyuki Terashima; Masafumi Koike; Seiji Kojima; Michio Homma
Journal:  J Bacteriol       Date:  2010-08-20       Impact factor: 3.490

6.  Release of flagellar filament-hook-rod complex by a Salmonella typhimurium mutant defective in the M ring of the basal body.

Authors:  H Okino; M Isomura; S Yamaguchi; Y Magariyama; S Kudo; S I Aizawa
Journal:  J Bacteriol       Date:  1989-04       Impact factor: 3.490

7.  Flagellar switch of Salmonella typhimurium: gene sequences and deduced protein sequences.

Authors:  M Kihara; M Homma; K Kutsukake; R M Macnab
Journal:  J Bacteriol       Date:  1989-06       Impact factor: 3.490

8.  Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus.

Authors:  M Kihara; T Minamino; S Yamaguchi; R M Macnab
Journal:  J Bacteriol       Date:  2001-03       Impact factor: 3.490

9.  Mass determination and estimation of subunit stoichiometry of the bacterial hook-basal body flagellar complex of Salmonella typhimurium by scanning transmission electron microscopy.

Authors:  G E Sosinsky; N R Francis; D J DeRosier; J S Wall; M N Simon; J Hainfeld
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-01       Impact factor: 11.205

10.  Basal-body-associated disks are additional structural elements of the flagellar apparatus isolated from Wolinella succinogenes.

Authors:  J Kupper; I Wildhaber; Z Gao; E Baeuerlein
Journal:  J Bacteriol       Date:  1989-05       Impact factor: 3.490

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