Factor analysis of interactions between alfalfa nodule bacteria (Sinorhizobium meliloti) genes that regulate symbiotic nitrogen fixation

• Published in: Genetika Vol. 49; no. 4; p. 448
• Main Authors: Provorov, N A, Chuklina, E, Vorob'ev, N I, Onishchuk, O P, Simarov, B V
• Format: Journal Article
• Language: Russian
• Published: Russia (Federation) 01.04.2013
• Subjects: Bacterial Proteins - genetics; Factor Analysis, Statistical; Gene Expression Regulation, Bacterial; Genes, Bacterial; Medicago sativa - microbiology; Medicago sativa - physiology; Nitrogen Fixation - genetics; Nitrogenase - genetics; PII Nitrogen Regulatory Proteins - genetics; Plant Roots - microbiology; Promoter Regions, Genetic; Sinorhizobium meliloti - genetics; Sinorhizobium meliloti - physiology; Symbiosis - genetics
• ISSN: 0016-6758
• DOI: 10.7868/S0016675813030156

Factor analysis has been conducted for the data on the interaction between the genes of the root nodule bacteria (rhizobia), which influence the efficiency of symbiosis with leguminous plants, including dctA (encoding succinate permease), dctBD (activating the dctA gene due to binding its enhancer in the presence of succinate), rpoN (activating the promoters of dctA and nitrogenase genes nifHDK), and nifA (activating the nitrogenase genes due to binding their enhancers). The analysis of the alfalfa rhizobia (Sinorhizobium meliloti) recombinants that contain additional copies ofthese genes suggested the antagonistic (epistatic) interaction between nifA and rpoN. It may be associated either with the competition for C compounds imported into the nodules between the energy production and nitrogen assimilation processes or with the competition for redox potentials between the oxidative phosphorylation and nitrogen fixation processes. Since the phenotypic effects of the studied genes depend on the activity of nitrogen export into the aerial parts of plants, we suppose that its accumulation in bacteroids impairs the activation of the nifHDK genes by the NifA protein due to its interaction with the GlnB protein (the nitrogen metabolism regulator) or with the FixLJ and ActSR proteins (the redox potential regulators).