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Genomics |
Dynamique des Membranes Végétales, Complexes Protéines-Pigments, CNRS UMR 8543, Ecole Normale Supérieure, 46 rue d’Ulm 75230 Paris Cedex 05, France1
Author for correspondence: Jean Houmard. Tel: +33 144323519. Fax: +33 144323935. e-mail: jhoumard{at}biologie.ens.fr
Cyanobacteria modulate intracellular levels of cAMP and cGMP in response to environmental conditions (light, nutrients and pH). In an attempt to identify components of the cAMP and cGMP signalling pathways in Synechocystis PCC 6803, the authors screened its complete genome sequence by using bioinformatic tools and data from sequence–function studies performed on both eukaryotic and prokaryotic cAMP/cGMP-dependent proteins. Sll1624 and Slr2100 were tentatively assigned as being two putative cyclic nucleotide phosphodiesterases. Five proteins were identified as having all the determinants required to be cyclic nucleotide receptors, two of them being probably more specific for cGMP (an element of two-component regulatory systems – Slr2104 – and a putative cyclic-nucleotide-gated cation channel – Slr1575), the three others being probably more specific for cAMP: (i) a protein of unidentified function (Slr0842); (ii) a putative cyclic-nucleotide-modulated permease (Slr0593), previously annotated as a kinase A regulatory subunit; and (iii) a putative transcription factor (CRP-Syn =Sll1371), which possesses cAMP- and DNA-binding determinants homologous to those of the cAMP receptor protein of Escherichia coli (CRP-Ec). This homology, together with the presence in Synechocystis of CRP-Ec-like binding sites upstream of crp, cya1, slr1575, and several genes encoding enzymes involved in transport and metabolism, strongly suggests that CRP-Syn is a global regulator.
Keywords: CRP, cyclic-nucleotide gated channel
Abbreviations: cNMP, cyclic nucleotide monophosphate; CNG, cyclic-nucleotide- gated; CRP, cAMP receptor protein
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