Dimerization of Rhizobium meliloti NifH protein in Saccharomyces cerevisiae cells requires simultaneous expression of NifM protein
| Autor: | Pencho Venkov, Liliana Gigova, Nina Petrova |
|---|---|
| Rok vydání: | 2001 |
| Předmět: |
Klebsiella pneumoniae
Macromolecular Substances Saccharomyces cerevisiae Genetic Vectors Gene Expression Biochemistry Enzyme Stability RNA Messenger Cloning Molecular Gene biology Molecular mass food and beverages Nitrogenase Cell Biology biochemical phenomena metabolism and nutrition biology.organism_classification Yeast Recombinant Proteins RNA Bacterial Genes Bacterial Protein Biosynthesis bacteria Rhizobium Diazotroph Oxidoreductases Dimerization Sinorhizobium meliloti |
| Zdroj: | The international journal of biochemistrycell biology. 34(1) |
| ISSN: | 1357-2725 |
| Popis: | Compared to free living diazotrophs, the nitrogenase system of symbiotic microorganisms, like Rhizobium (Synorhizobium) meliloti, was poorly studied. The aim of our research was to investigate whether (by analogy with Klebsiella pneumoniae) the NifM product is required and sufficient to obtain active R. meliloti Fe-protein. We cloned nifH gene of R. meliloti and nifM gene of K. pneumoniae in suitable yeast vectors. When introduced into Saccharomyces cerevisiae cells, both genes were effectively expressed to proteins similar to the native products in its immunoreactivity and apparent molecular mass. The association of R. meliloti NifH protein into dimer structure required co-expression of NifM that also conferred stability of NifH polypeptide. However, the NifH protein synthesized in yeast did not show enzyme activity, suggesting that the NifM of K. pneumoniae is incapable of activating the NifH protein of R. meliloti. |
| Databáze: | OpenAIRE |
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