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Citation
Biswas, K.H., Shenoy, A.R., Dutta, A., Visweswariah, S.S. (2009). The evolution of guanylyl cyclases as multidomain proteins: conserved features of kinase-cyclase domain fusions.  J. Mol. Evol. 68(6): 587--602.
FlyBase ID
FBrf0228387
Publication Type
Research paper
Abstract

Guanylyl cyclases (GCs) are enzymes that generate cyclic GMP and regulate different physiologic and developmental processes in a number of organisms. GCs possess sequence similarity to class III adenylyl cyclases (ACs) and are present as either membrane-bound receptor GCs or cytosolic soluble GCs. We sought to determine the evolution of GCs using a large-scale bioinformatic analysis and found multiple lineage-specific expansions of GC genes in the genomes of many eukaryotes. Moreover, a few GC-like proteins were identified in prokaryotes, which come fused to a number of different domains, suggesting allosteric regulation of nucleotide cyclase activity. Eukaryotic receptor GCs are associated with a kinase homology domain (KHD), and phylogenetic analysis of these proteins suggest coevolution of the KHD and the associated cyclase domain as well as a conservation of the sequence and the size of the linker region between the KHD and the associated cyclase domain. Finally, we also report the existence of mimiviral proteins that contain putative active kinase domains associated with a cyclase domain, which could suggest early evolution of the fusion of these two important domains involved in signal transduction.

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    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    J. Mol. Evol.
    Title
    Journal of Molecular Evolution
    Publication Year
    1971-
    ISBN/ISSN
    0022-2844
    Data From Reference
    Gene Groups (2)
    Genes (8)