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Originally published as MBC in Press, 10.1091/mbc.E02-05-0302 on September 24, 2002
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Vol. 13, Issue 11, 3878-3889, November 2002

Identification and Characterization of Two Unusual cGMP-stimulated Phoshodiesterases in Dictyostelium

Leonard Bosgraaf, Henk Russcher, Helena Snippe, Sonya Bader, Joyce Wind, and Peter J.M. Van Haastert*

Department of Biochemistry, University of Groningen, 9747 AG Groningen, The Netherlands

Recently, we recognized two genes, gbpA and gbpB, encoding putative cGMP-binding proteins with a Zn2+-hydrolase domain and two cyclic nucleotide binding domains. The Zn2+-hydrolase domains belong to the superfamily of beta -lactamases, also harboring a small family of class II phosphodiesterases from bacteria and lower eukaryotes. Gene inactivation and overexpression studies demonstrate that gbpA encodes the cGMP-stimulated cGMP-phosphodiesterase that was characterized biochemically previously and was shown to be involved in chemotaxis. cAMP neither activates nor is a substrate of GbpA. The gbpB gene is expressed mainly in the multicellular stage and seems to encode a dual specificity phosphodiesterase with preference for cAMP. The enzyme hydrolyses cAMP ~9-fold faster than cGMP and is activated by cAMP and cGMP with a KA value of ~0.7 and 2.3 µM, respectively. Cells with a deletion of the gbpB gene have increased basal and receptor stimulated cAMP levels and are sporogeneous. We propose that GbpA and GbpB hydrolyze the substrate in the Zn2+-hydrolase domain, whereas the cyclic nucleotide binding domains mediate activation. The human cGMP-stimulated cAMP/cGMP phosphodiesterase has similar biochemical properties, but a completely different topology: hydrolysis takes place by a class I catalytic domain and GAF domains mediate cGMP activation.

* Corresponding author. E-mail address: p.j.m.van.haastert{at}chem.rug.nl.

Molecular Biology of the Cell
Vol. 13, 3878-3889, November 2002
Copyright © 2002 by The American Society for Cell Biology


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