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Chemomechanical coupling without ATP: the source of energy for motility and chemotaxis in bacteria.

Author information

Affiliations

  • 1. Department of Biochemistry, University of Wisconsin, Madison, Wis. 53706
      Authors
    • Larsen SH 1
    • Adler J 1
    (2 authors)
  • 2. Department of Microbiology, Case Western Reserve University, Cleveland, Ohio 44106
      Authors
    • Gargus JJ 2
    • Hogg RW 2
    (2 authors)

Proceedings of the National Academy of Sciences of the United States of America, 01 Apr 1974, 71(4):1239-1243
https://doi.org/10.1073/pnas.71.4.1239 PMID: 4598295 PMCID: PMC388200

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Abstract 

The source of energy for bacterial motility is the intermediate in oxidative phosphorylation, not ATP directly. For chemotaxis, however, there is an additional requirement, presumably ATP. These conclusions are based on the following findings. (i) Unlike their parents, mutants of Escherichia coli and Salmonella typhimurium that are blocked in the conversion of ATP to the intermediate of oxidative phosphorylation failed to swim anaerobically, even when they produced ATP. When respiration was restored to the mutants, motility was simultaneously restored. (ii) Carbonylcyanide m-chlorophenylhydrazone, which uncouples oxidative phosphorylation, completely inhibited motility even though ATP remained present. (iii) Arsenate did not inhibit motility in the presence of an oxidizable substrate, though it did reduce ATP levels to less than 0.3% (iv) Arsenate completely inhibited chemotaxis under conditions where motility was normal.

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Proc Natl Acad Sci U S A. 1974 Apr; 71(4): 1239–1243.
PMCID: PMC388200
PMID: 4598295

Chemomechanical Coupling without ATP: The Source of Energy for Motility and Chemotaxis in Bacteria

Steven H. Larsen,* Julius Adler,†‡ J. Jay Gargus,§ and Robert W. Hogg§
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Abstract

The source of energy for bacterial motility is the intermediate in oxidative phosphorylation, not ATP directly. For chemotaxis, however, there is an additional requirement, presumably ATP. These conclusions are based on the following findings. (i) Unlike their parents, mutants of Escherichia coli and Salmonella typhimurium that are blocked in the conversion of ATP to the intermediate of oxidative phosphorylation failed to swim anaerobically, even when they produced ATP. When respiration was restored to the mutants, motility was simultaneously restored. (ii) Carbonylcyanide m-chlorophenylhydrazone, which uncouples oxidative phosphorylation, completely inhibited motility even though ATP remained present. (iii) Arsenate did not inhibit motility in the presence of an oxidizable substrate, though it did reduce ATP levels to less than 0.3% (iv) Arsenate completely inhibited chemotaxis under conditions where motility was normal.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
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