The regulation of flagellar formation and function

Hilmen, Marcia; Silverman, Melvin

doi:10.1002/jss.400020225

Cited by 31 publications

(19 citation statements)

References 30 publications

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“…To identify the triplet protein with one of the polypeptides involved in flagellar structure or function, it was compared to the polypeptide component of the flagellar basal structure which has an apparent molecular weight of 59,000 on acrylamide gels (7) and to the MCP described by Kort et al (9) which has also been reported to have an apparent molecular weight of 60,000. These radioactive polypeptides were compared by polyacrylamide gel electrophoresis under a variety of conditions.…”

Section: Resultsmentioning

confidence: 99%

Characterization of lambda Escherichia coli hybrids carrying chemotaxis genes

Silverman¹,

Matsumura²,

Hilmen³

et al. 1977

J Bacteriol

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Molecular cloning techniques were used to construct hybrid Escherichia coli lambda phage and isolate Col El factors that carried the cheB region of the E. coli genome. The products of these genes were examined by using a series of deletions in the phage to stimulate specific polypeptide synthesis in ultravioletirradiated cells and by using Col factor to program protein synthesis in minicells. Seven flagellar related polypeptides were synthesized. Three of these with apparent molecular weights of 38,000, 28,000, and 8,000 were associated with the cheB region; three polypeptides 63,000, 61,000, and 60,000 were associated with the region that maps between cheB and cheA. These bands were referred to as the triplet group. We suggest that these polypeptides are the same as the methyl-accepting chemotaxis protein described by Kort et al. (Proc. Natl. Acad. Sci. U.S.A. 72:3939-3943, 1975). Another polypeptide with a molecular weight of 12,000 is associated with the cheA region which also produces at least three gene products. We conclude that the cheA-cheB region in E. coli is complex. Further genetic and biochemical analyses are required to describe all of these products.

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Section: Resultsmentioning

confidence: 99%

Characterization of lambda Escherichia coli hybrids carrying chemotaxis genes

Silverman¹,

Matsumura²,

Hilmen³

et al. 1977

J Bacteriol

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“…It has been unclear whether the target of the glucose effect is flagellin synthesis or some step in flagella assembly. Recently a mutant of E coli, eft, has been isolated, which releases flagella fo rmation from catabolite repression (57,154), and the phenotype of this mutant has led Silverman and Simon to suggest that flagella structural proteins are catabolically repressed either directly or indirectly. In contrast to the inhibitory effect of 10 mM glucose on flagella fo rmation in E. coli and S. typh imurium, glucose (up to 0.1 M) does not inhibit flageJla fo rmation or motility in C crescentus grown on defined minimal Annu.…”

Section: Flagella and Pili Biogenesismentioning

confidence: 98%

DIFFERENTIATION IN THE CAULOBACTER CELL CYCLE

Shapiro¹

1976

Annu. Rev. Microbiol.

110

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“…It is composed of a long helical filament and a complex basal structure which is tightly bound to the outer membrane of the cell. The basal structure has been purified (9) and its components were characterized by gel electrophoresis. It was found to contain eleven different polypeptide chains (10).…”

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confidence: 99%

The identification of the mot gene product with Escherichia coli-lambda hybrids.

Silverman¹,

Matsumura²

1976

Proc. Natl. Acad. Sci. U.S.A.

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Molecular cloning techniques were used to construct lambda-E. coli hybrid bacteriophage carrying genes involved in bacterial flagellar motility (mot) and chemotaxis (cheA). A series of hybrid bacteriophage without each of these genes was also prepared. When paralyzed mutants of E. coli were infected with lambda that carried the mot gene, the ability of the bacterium to swim was rapidly restored. The restoration of motility was the result of the synthesis and insertion into the cell membrane of a protein with an apparent molecular weight of 31,000 (the Mot protein).Another polypeptide with a mobility on acrylamide gel electrophoresis which corresponded to a molecular weight of 39,000 was associated with the cheA gene. The presence of this polypeptide alone was not sufficient to restore chemotactic activity to mutant cheA strains. It was suggested that only a portion of the cheA gene was cloned, and thus the 39,000 protein may be a partial product of the cheA gene, or the product of a second mot gene.Bacterial flagella function by rotating, and their rotation is regulated so that it responds to information provided by specific chemoreceptors on the surface of the cell (1-3). The genetic basis for flagellar structure, function, and regulation has been analyzed in detail (4-6). However, very little is known about the biochemistry involved in these processes. The flagellar organelle can be isolated from Escherichia coli and Bacillus subtilis (7,8). It is composed of a long helical filament and a complex basal structure which is tightly bound to the outer membrane of the cell. The basal structure has been purified (9) and its components were characterized by gel electrophoresis. It was found to contain eleven different polypeptide chains (10). It is clear, however, that these components do not account for all of the gene products involved in flagellar function. This conclusion is based on a comparison of the proteins obtained from flagella isolated from mot amber mutants and wild-type strains. The mot gene appears to control the synthesis of a product which is directly involved in flagellar activity. Mutations in (16,17).To understand the mechanisms involved in motility, and in the assembly and function of flagella, it is necessary to identify the products of all of the genes that contribute to these processes.One approach involves an isolation of the genes and detection of their products directly. In a previous report (18), we showed that hybrid E. coli-lambda phage carrying genes that control flagellin synthesis could be obtained and used to determine the regulation of flagellin production. We will now show how hybrid lambda bacteriophage can be used to assay for other flagella-specific proteins which include the mot gene product. MATERIALS AND METHODSConstruction and Propagation of Hybrid Lambda. Hybrid lambda (X) E. coli DNA molecules were constructed using XgtXc DNA as the vehicle and fragments of DNA obtained by EcoRI endonuclease digestion of F factor carrying flagellar genes. The isolation of the F ...

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The regulation of flagellar formation and function

Cited by 31 publications

References 30 publications

Characterization of lambda Escherichia coli hybrids carrying chemotaxis genes

Characterization of lambda Escherichia coli hybrids carrying chemotaxis genes

DIFFERENTIATION IN THE CAULOBACTER CELL CYCLE

The identification of the mot gene product with Escherichia coli-lambda hybrids.

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