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A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria

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Abstract

Many biological processes are coupled to ATP hydrolysis. We describe here a class of closely related ATP-binding proteins, from several bacterial species, which are associated with a variety of cellular functions including membrane transport, cell division, nodulation in Rhizobium and haemolysin export. These proteins comprise a family of structurally and functionally related subunits which share a common evolutionary origin, bind ATP and probably serve to couple ATP hydrolysis to each of these biological processes. This finding suggests a specific role for ATP in cell division, nodulation during nitrogen fixation and protein export, and allows us to assign a probable function to one of the protein components from each of these systems.

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Author notes

  1. George P. C. Salmond and Deborah R. Gill: Department of Biological Sciences, University of Warwick, Coventry CV4 7AL, UK

  2. J. Allan Downie and Ian J. Evans: John Innes Institute, Colney Lane, Norwich NR4 7UH, UK

  3. I. Barry Holland and Lindsay Gray: Department of Genetics, University of Leicester, Leicester LE1 7RH, UK

  4. Scott D. Buckel, Alexander W. Bell and Mark A. Hermodson: Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, USA

Authors and Affiliations

  1. Molecular Genetics Laboratory, Department of Biochemistry, University of Dundee, Dundee, DD1 4HN, UK

    Christopher F. Higgins, Ian D. Hiles, George P. C. Salmond, Deborah R. Gill, J. Allan Downie, Ian J. Evans, I. Barry Holland, Lindsay Gray, Scott D. Buckel, Alexander W. Bell & Mark A. Hermodson

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  1. Christopher F. Higgins
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  2. Ian D. Hiles
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  3. George P. C. Salmond
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  4. Deborah R. Gill
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  5. J. Allan Downie
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  6. Ian J. Evans
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  7. I. Barry Holland
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  8. Lindsay Gray
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  9. Scott D. Buckel
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  10. Alexander W. Bell
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  11. Mark A. Hermodson
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Higgins, C., Hiles, I., Salmond, G. et al. A family of related ATP-binding subunits coupled to many distinct biological processes in bacteria. Nature 323, 448–450 (1986). https://doi.org/10.1038/323448a0

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  • DOI: https://doi.org/10.1038/323448a0

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