Modulation of PQQ-dependent glucose dehydrogenase (mGDH and sGDH) activity by succinate in phosphate solubilizing plant growth promoting Acinetobacter sp. SK2

Prospective plant growth promoting rhizobacteria isolated from the rhizosphere of Vigna radiata was identified as Acinetobacter sp. SK2 that solubilized 682 μg ml⁻¹ of tricalcium phosphate (TCP) and 86 μg ml⁻¹ of rock phosphate (RP) with concomitant decrease in pH up to 4 due to the production of gluconate. The biochemical basis of the P solubilization suggested that the gluconate production was mediated by mGDH and sGDH enzymes. Our results illustrate the role of succinate in repression of P solubilization via suppression of mGDH and sGDH activity which correlated with repression of expression of respective genes, gdhA and gdhB. SK2 also produced IAA (117 μg ml⁻¹), siderophore (87% units), HCN, ammonia and solubilized minerals of Zn and K. Our findings imply that it is important to understand the cause of failure of several phosphate solubilizing bacteria in field conditions where catabolite repression may control the expression of several genes and pathways including that of mineral phosphate solubilization. Furthermore, Acinetobacter sp. SK2 bearing two glucose dehydrogenase (gdhA and gdhB) genes was recognized as promising strain for P biofortification and enhanced plant growth promotion.