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A more recent version of this article appeared on November 1, 2002
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Submitted on May 16, 2002
Revised on July 8, 2002
Accepted on August 19, 2002
1 School of Life Sciences, University of Dundee, MSI/WTB complex, Dow Street, Dundee DD1 5EH, UK
* Corresponding author. E-mail address: p.schaap{at}dundee.ac.uk.
StmF mutants are chemotactic mutants that are defective in a cGMP phosphodiesterase(PDE) activity. We identified a novel gene, PdeD, which harbours two cyclic nucleotide binding domains and a metallo-ß-lactamase homology domain. Similar to stmF mutants, pdeD null mutants displayed extensively streaming aggregates, prolonged elevation of cGMP levels after chemotactic stimulation and reduced cGMP-PDE activity. PdeD transcripts were lacking in stmF mutant NP377, indicating that this mutant carries a PdeD lesion. Expression of a PdeD-YFP fusion protein in pdeD null cells restored the normal cGMP response and showed that PdeD resides in the cytosol. When purified by immunoprecipitation, the PdeD-YFP fusion protein displayed cGMP-PDE activity, which was retained in a truncated construct that contained only the metallo-ß-lactamase domain.
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