Sucrose dependent mineral phosphate solubilization in Enterobacter asburiae PSI3 by heterologous overexpression of periplasmic invertases

2016 ◽  
Vol 32 (12) ◽  
Author(s):  
Chanchal Kumar ◽  
Jitendra Wagh ◽  
G. Archana ◽  
G. Naresh Kumar
Keyword(s):  
Phosphate Solubilization ◽  
Mineral Phosphate Solubilization ◽  
Heterologous Overexpression ◽  
Mineral Phosphate ◽  
Enterobacter Asburiae

scholarly journals Characterization of mineral phosphate solubilization traits from a barley rhizosphere soil functional metagenome

2013 ◽  
Vol 2 (5) ◽  
pp. 717-724 ◽  
Author(s):  
Sagar Chhabra ◽  
Dina Brazil ◽  
John Morrissey ◽  
James I. Burke ◽  
Fergal O'Gara ◽  
...  
Keyword(s):  
Rhizosphere Soil ◽  
Phosphate Solubilization ◽  
Mineral Phosphate Solubilization ◽  
Mineral Phosphate

Highly Conserved Asp-204 and Gly-776 Are Important for Activity of the Quinoprotein Glucose Dehydrogenase of Escherichia coli and for Mineral Phosphate Solubilization

2010 ◽  
Vol 18 (2) ◽  
pp. 109-119 ◽  
Author(s):  
Burla Sashidhar ◽  
Krishna Kishore Inampudi ◽  
Lalitha Guruprasad ◽  
Anil Kondreddy ◽  
Kodetham Gopinath ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Phosphate Solubilization ◽  
Glucose Dehydrogenase ◽  
Mineral Phosphate Solubilization ◽  
Mineral Phosphate

scholarly journals Crc Regulates Succinate-Mediated Repression of Mineral Phosphate Solubilization in Acinetobacter sp. SK2 by Modulating Membrane Glucose Dehydrogenase

2021 ◽  
Vol 12 ◽  
Author(s):  
Krishna Bharwad ◽  
Niharika Ghoghari ◽  
Shalini Rajkumar
Keyword(s):  
Glucose Oxidation ◽  
Phosphate Solubilization ◽  
Glucose Dehydrogenase ◽  
Carbon Sources ◽  
Shoot Length ◽  
Wild Type ◽  
Mineral Phosphate Solubilization ◽  
Root And Shoot Length ◽  
Mineral Phosphate ◽  
Encoding Gene

The plant growth-promoting Acinetobacter sp. SK2 isolated from Vigna radiata rhizosphere was characterized for mineral phosphate solubilization (MPS). To understand the contribution of the membrane glucose dehydrogenase (mGDH) and soluble glucose dehydrogenase (sGDH) in glucose oxidation and MPS, insertional inactivation of the corresponding genes was carried out. The disruption of mGDH encoding gene gdhA resulted in complete loss of mGDH activity, which confirmed its role in periplasmic glucose oxidation and gluconate-mediated MPS phenotype. The inactivation of sGDH encoding gene gdhB resulted in loss of sGDH activity, which did not alter the MPS or mGDH activity. Thus, it was also concluded that the sGDH was dispensable in gluconate-mediated MPS. Supplementation of succinate in glucose-containing medium suppressed the activity of mGDH (and sGDH) and therefore repressed the MPS phenotype. The catabolite repression control protein (Crc) of Pseudomonas was implicated in Acinetobacter sp. for a similar function in the presence of preferred and non-preferred carbon sources. To understand the regulatory linkage between Crc and genes for glucose oxidation, crc mutants were generated. The inactivation of crc resulted in increased activity of the mGDH in glucose + succinate-grown cells, indicating derepression. An increase in phosphate solubilization up to 44% in glucose + succinate-grown crc– compared with glucose-grown cells was recorded, which was significantly repressed in the wild-type strain under similar conditions. It is therefore proposed that in Acinetobacter sp. SK2, Crc is involved in the succinate-provoked repression of the MPS phenotype. The gene expression data indicated that Hfq may also have a regulating role in preferential utilization of carbon source by perhaps modulating Crc–Hfq functionality. V. radiata plants inoculated with the wild type improved both root and shoot length by 1.3 to 1.4-fold. However, crc– increased the root and shoot length by 1.6-fold, compared with the uninoculated controls. In mimicking the soil condition (in the presence of multiple carbon sources, e.g., succinate along with glucose), the crc– strain of Acinetobacter sp. SK2 performed better in supporting the growth of V. radiata in pot experiments.

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