Arginine kinase in the demosponge Suberites domuncula:regulation of its expression and catalytic activity by silicic acid
| Autor: | Renato Batel, Isabel M. Müller, Marco Giovine, Matthias Wiens, Anatoli Krasko, Sanja Perović-Ottstadt, H. C. Schröder, Werner E.G. Müller |
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| Rok vydání: | 2005 |
| Předmět: |
DNA
Complementary Arginine Physiology Molecular Sequence Data Silicic Acid Aquatic Science Catalysis Gene Expression Regulation Enzymologic Evolution Molecular chemistry.chemical_compound Demosponge Microscopy Electron Transmission Animals Cluster Analysis Amino Acid Sequence Northern blot Silicic acid Molecular Biology In Situ Hybridization Phylogeny Ecology Evolution Behavior and Systematics chemistry.chemical_classification Base Sequence biology Kinase Arginine Kinase Sequence Analysis DNA Arginine kinase Blotting Northern biology.organism_classification Porifera Suberites domuncula Enzyme chemistry Biochemistry Insect Science biology.protein Animal Science and Zoology Sequence Alignment |
| Zdroj: | Journal of Experimental Biology. 208:637-646 |
| ISSN: | 1477-9145 0022-0949 |
| DOI: | 10.1242/jeb.01428 |
| Popis: | SUMMARY In Demospongiae (phylum Porifera) the formation of the siliceous skeleton,composed of spicules, is an energetically expensive reaction. The present study demonstrates that primmorphs from the demosponge Suberites domuncula express the gene for arginine kinase after exposure to exogenous silicic acid. The deduced sponge arginine kinase sequence displays the two characteristic domains of the ATP:guanido phosphotransferases; it can be grouped to the `usual' mono-domain 40 kDa guanidino kinases (arginine kinases). Phylogenetic studies indicate that the metazoan guanidino kinases evolved from this ancestral sponge enzyme; among them are also the `unusual'two-domain 80 kDa guanidino kinases. The high expression level of the arginine kinase gene was already measurable 1 day after addition of silicic acid by northern blot, as well as by in situ hybridization analysis. Parallel determinations of enzyme activity confirmed that high levels of arginine kinase are present in primmorphs that had been exposed for 1-5 days to silicic acid. Finally, transmission electron-microscopical studies showed that primmorphs containing high levels of arginine kinase also produce siliceous spicules. These data highlight that silicic acid is an inorganic morphogenetic factor that induces the expression of the arginine kinase, which in turn probably catalyzes the reversible transfer of high-energy phosphoryl groups. |
| Databáze: | OpenAIRE |
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