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Originally published as MBC in Press, 10.1091/mbc.E02-05-0285 on September 24, 2002
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Vol. 13, Issue 11, 3870-3877, November 2002

Identification of a Novel Type of cGMP Phosphodiesterase That Is Defective in the Chemotactic stmF Mutants

Marcel E. Meima, Ricardo M. Biondi, and Pauline Schaap*

School of Life Sciences, University of Dundee, Dundee DD1 5EH, United Kingdom.

StmF mutants are chemotactic mutants that are defective in a cGMP phosphodiesterase (PDE) activity. We identified a novel gene, PdeD, that harbors two cyclic nucleotide-binding domains and a metallo-beta -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-beta -lactamase domain.

* Corresponding author. E-mail address: p.schaap{at}dundee.ac.uk.

Molecular Biology of the Cell
Vol. 13, 3870-3877, November 2002
Copyright © 2002 by The American Society for Cell Biology


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