A single amino acid substitution responsible for altered flagellar morphology

Martı́nez, Rafael; Ichiki, Albert T.; Lundh, Nancy P.; Tronick, Steven R.

doi:10.1016/0022-2836(68)90180-0

Cited by 48 publications

(24 citation statements)

References 15 publications

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“…This is consistent with the observation that a single amino acid change in FliC resulted in improper assembly or export of unassembled flagellin into the surrounding growth medium (21). Furthermore, other terminal-region mutations have been reported to result in straight, nonfunctional filaments (21,31). An alignment of the N-terminal 190 amio acids of known enterobacterial FliC proteins (Fig.…”

Section: Methodssupporting

confidence: 88%

Comparative analysis of flagellin sequences from Escherichia coli strains possessing serologically distinct flagellar filaments with a shared complex surface pattern

Schoenhals

Whitfield

1993

J Bacteriol

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ence of both serotype-specific determinants (3,16,19,20,39,43,60) and cross-reactive determinants (1,3,5,12,13,26,43). The immunological relationships among morphotype E flagellins have been analyzed by using monoclonal antibodies (43,60). In addition to serotype-specific and broadly cross-reactive epitopes, other epitopes were common among subgroups of closely related flagellin serotypes within morphotype E. Immunogold labeling studies demonstrated that serotype-specific determinants tend to be surface exposed in intact flagellar filaments, while cross-reactive determinants tend to be hidden (43,60).DNA sequence analysis of flagellin structural genes from E. coli K-12 (24), Serratia marcescens (10), and several Salmonella serovars (15,48,58,59) demonstrated that the termini of flagellin proteins are conserved. The central region of the flagellin molecule is variable and gives rise to serotype-specific epitopes (6,16,18,19,23,36,45,47,48,58). The flagellin protein therefore possesses several distinct structural domains (34,46,(51)(52)(53)(54)56). These have been mapped on the primary structure of the flagellin molecule and localized within the intact flagellar filament by electron density mapping studies (57). The conserved, terminal regions of flagellin were found to be associated with the inner structure of intact flagellar filaments. The outer surfaceexposed architecture is formed from the folding outward of 5395

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Section: Methodssupporting

confidence: 88%

Comparative analysis of flagellin sequences from Escherichia coli strains possessing serologically distinct flagellar filaments with a shared complex surface pattern

Schoenhals

Whitfield

1993

J Bacteriol

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“…This discrepancy is most likely due to an error in the sequencing of the flagellin protein, since the nucleotide sequence of the flagellin gene was determined from both DNA strands. Such an alteration of the primary sequence of the B. subtilis flagellin protein would not significantly affect previous comparative analyses of bacterial flagellin protein structure (9,24,29,33,35 (28,38).…”

Section: Resultsmentioning

confidence: 97%

The Bacillus subtilis flagellin gene (hag) is transcribed by the sigma 28 form of RNA polymerase

1989

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The Bacillus subtilis gene hag, which codes for the flagellin structural protein, was identified by DNA sequence analysis in a collection of DNA fragments bearing in vitro promoters for the c28 form of RNA polymerase. The hag gene and adjacent, regions of the B. subtilis chromosome were restriction mapped, and the nucleotide sequence was determined. The hag gene was transcribed at all stages of growth from a single promoter that had sequences in the promoter recognition region characteristic of the consensus sequence for the o28 holoenzyme. Transcription of hag was elinminated by insertion mutations that blocked synthesis of the I28 protein. These findings provide strong support for the previous proposal that the Cr28 form of RNA polymerase controls transcription of a regulon specifying flagellar, chemotaxis, and motility functions in B. subtilis (J. D. Helmann and M. J. Chamberlin, Proc. Natl. Acad. Sci. USA 84:6422-6424, 1987). The steady-state levels of hag mRNA increased during exponential growth and peaked as the B. subtilis cells entered the stationary phase. The transcript levels then decreased to zero within 4 h after the onset of sporulation. Hence, cr28 RNA polymerase function is temporally regulated.

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“…Amino acid exchange in flagellin is known to influence flagellar morphology and mobility. An alanine-to-valine mutation in Bacillus subtilis 168 causes a straight flagellum phenotype and the loss of motility (29). E. coli strain W3623 (ha-177) that produces straight flagella does not swarm in 0.35% semisolid agar (24).…”

Section: Discussionmentioning

confidence: 99%

Three Mutations in Escherichia coli That Generate Transformable Functional Flagella

et al. 2012

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bHydrodynamics predicts that swimming bacteria generate a propulsion force when a helical flagellum rotates because rotating helices necessarily translate at a low Reynolds number. It is generally believed that the flagella of motile bacteria are semirigid helices with a fixed pitch determined by hydrodynamic principles. Here, we report the characterization of three mutations in laboratory strains of Escherichia coli that produce different steady-state flagella without losing cell motility. E. coli flagella rotate counterclockwise during forward swimming, and the normal form of the flagella is a left-handed helix. A single amino acid exchange A45G and a double mutation of A48S and S110A change the resting flagella to righthanded helices. The stationary flagella of the triple mutant were often straight or slightly curved at neutral pH. Deprotonation facilitates the helix formation of it. The helical and curved flagella can be transformed to the normal form by torsion upon rotation and thus propel the cell. These mutations arose in the long-term laboratory cultivation. However, flagella are under strong selection pressure as extracellular appendages, and similar transformable flagella would be common in natural environments.

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A single amino acid substitution responsible for altered flagellar morphology

Cited by 48 publications

References 15 publications

Comparative analysis of flagellin sequences from Escherichia coli strains possessing serologically distinct flagellar filaments with a shared complex surface pattern

Comparative analysis of flagellin sequences from Escherichia coli strains possessing serologically distinct flagellar filaments with a shared complex surface pattern

The Bacillus subtilis flagellin gene (hag) is transcribed by the sigma 28 form of RNA polymerase

Three Mutations in Escherichia coli That Generate Transformable Functional Flagella

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