CyaG, a Novel Cyanobacterial Adenylyl Cyclase and a Possible Ancestor of Mammalian Guanylyl Cyclases
| Autor: | Tsuyoshi Unno, Masahiro Kasahara, Kumiko Yashiro, Masayuki Ohmori |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Recombinant Fusion Proteins
Molecular Sequence Data Cyanobacteria Biochemistry ADCY10 Evolution Molecular Adenylyl cyclase chemistry.chemical_compound Catalytic Domain Escherichia coli Animals Amino Acid Sequence Cloning Molecular Molecular Biology Peptide sequence Conserved Sequence Phylogeny Glutathione Transferase ADCY6 ADCY5 Base Sequence Models Genetic Sequence Homology Amino Acid ADCY9 Sequence Analysis DNA Cell Biology ADCY3 Protein Structure Tertiary chemistry Guanylate Cyclase Mutation Mutagenesis Site-Directed GUCY2D Dimerization Adenylyl Cyclases Plasmids |
| Zdroj: | Journal of Biological Chemistry. 276:10564-10569 |
| ISSN: | 0021-9258 |
| DOI: | 10.1074/jbc.m008006200 |
| Popis: | A novel gene encoding an adenylyl cyclase, designated cyaG, was identified in the filamentous cyanobacterium Spirulina platensis. The predicted amino acid sequence of the C-terminal region of cyaG was similar to the catalytic domains of Class III adenylyl and guanylyl cyclases. The N-terminal region next to the catalytic domain of CyaG was similar to the dimerization domain, which is highly conserved among guanylyl cyclases. As a whole, CyaG is more closely related to guanylyl cyclases than to adenylyl cyclases in its primary structure. The catalytic domain of CyaG was expressed in Escherichia coliand partially purified. CyaG showed adenylyl cyclase (but not guanylyl cyclase) activity. By site-directed mutagenesis of three amino acid residues (Lys533, Ile603, and Asp605) within the purine ring recognition site of CyaG to Glu, Arg, and Cys, respectively, CyaG was transformed to a guanylyl cyclase that produced cGMP instead of cAMP. Thus having properties of both cyclases, CyaG may therefore represent a critical position in the evolution of Class III adenylyl and guanylyl cyclases. |
| Databáze: | OpenAIRE |
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