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Polyphosphates from Mycobacterium bovis - potent inhibitors of class III adenylate cyclases

Lookup NU author(s): Professor Waldemar Vollmer


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cAMP generation in bacteria is often stimulated by sudden, but lasting, changes in extracellular conditions, whereas intracellular cAMP concentrations quickly settle at new levels. As bacteria lack G-proteins, it is unknown how bacterial adenylate cyclase (AC) activities are modulated. Mycobacterium tuberculosis has 15 class III AC genes; therefore, we examined whether mycobacteria contain a factor that may regulate AC activities. We identified mycobacterial polyphosphates with a mean chain length of 72 residues as highly potent inhibitors of dimeric class IIIa, class IIIb and class IIIc ACs from M. tuberculosis and other bacteria. The identity of the inhibitor was established by phosphatase degradation, 31P-NMR, acid or base hydrolysis, PAGE and comparisons with commercial standards, and functional substitution by several polyphosphates. The data indicate that each AC dimer occupies 8–15 phosphate residues on a polyphosphate strand. Other polyionic polymers such as polyglutamate, polylysine and hyaluronic acid do not affect cyclase activity. Notably, the structurally unrelated class I AC Cya from Escherichia coli is unaffected. Bacterial polyphosphate metabolism is generally viewed in the context of stress-related regulatory networks. Thus, regulation of bacterial class III ACs by polyphosphates could be a component of the bacterial stress response.

Publication metadata

Author(s): Guo YL, Mayer H, Vollmer W, Dittrich D, Sander P, Schultz A, Schultz JE

Publication type: Article

Publication status: Published

Journal: FEBS Journal

Year: 2009

Volume: 276

Issue: 4

Pages: 1094-1103

ISSN (print): 1742-464X

ISSN (electronic): 1742-4658

Publisher: Wiley-Blackwell Publishing Ltd.


DOI: 10.1111/j.1742-4658.2008.06852.x


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Funder referenceFunder name
3100A0_120326Swiss National Science Foundation
LSHP-CT-2006-037217European Union
SFB 766Deutsche Forschungsgemeinschaft