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Journal of Bacteriology, December 2000, p. 6687-6693, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Inorganic Polyphosphate in Vibrio cholerae: Genetic, Biochemical, and Physiologic Features

Nobuo Ogawa, Chi-Meng Tzeng, Cresson D. Fraley, and Arthur Kornberg^*

Department of Biochemistry, Stanford University School of Medicine, Stanford, California 94305-5307

Received 12 May 2000/Accepted 8 September 2000

Vibrio cholerae O1, biotype El Tor, accumulates inorganic polyphosphate (poly P) principally as large clusters of granules. Poly P kinase (PPK), the enzyme that synthesizes poly P from ATP, is encoded by the ppk gene, which has been cloned from V. cholerae, overexpressed, and knocked out by insertion-deletion mutagenesis. The predicted amino acid sequence of PPK is 701 residues (81.6 kDa), with 64% identity to that of Escherichia coli, which it resembles biochemically. As in E. coli, ppk is part of an operon with ppx, the gene that encodes exopolyphosphatase (PPX). However, unlike in E. coli, PPX activity was not detected in cell extracts of wild-type V. cholerae. The ppk null mutant of V. cholerae has diminished adaptation to high concentrations of calcium in the medium as well as motility and abiotic surface attachment.

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^* Corresponding author. Mailing address: Department of Biochemistry, Beckman Center, Stanford University School of Medicine, Stanford, CA 94305-5307. Phone: (650) 723-6167. Fax: (650) 723-6783. E-mail: akornber{at}cmgm.stanford.edu.

Present address: Institute of BioAgricultural Science, Academia Sinica, Nankang, Taiwan.

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Journal of Bacteriology, December 2000, p. 6687-6693, Vol. 182, No. 23
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

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