Browse by author
Lookup NU author(s): Professor Waldemar Vollmer
Full text for this publication is not currently held within this repository. Alternative links are provided below where available.
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.
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.
URL: http://dx.doi.org/10.1111/j.1742-4658.2008.06852.x
DOI: 10.1111/j.1742-4658.2008.06852.x
Altmetrics provided by Altmetric
