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Maize rhizosphere in Sichuan, China, hosts plant growth promoting Burkholderia cepacia with phosphate solubilizing and antifungal abilities

文献类型： 外文期刊

作者： Zhao, Ke 1 ; Penttinen, Petri 2 ; Zhang, Xiaoping 1 ; Ao, Xiaoling 1 ; Liu, Maoke 3 ; Yu, Xiumei 1 ; Chen, Qiang 1 ;

作者机构： 1.Sichuan Agr Univ, Dept Microbiol, Coll Resource & Environm Sci, Yaan 625000, Peoples R China

2.Univ Helsinki, Dept Food & Environm Sci, FIN-00014 Helsinki, Finland

3.Sichuan Acad Agr Sci, Ctr Biotechnol, Rice & Sorghum Res Inst, Luzhou 646100, Peoples R China

关键词： Plant growth-promoting rhizobacteria;Phosphate solubilizing bacterial;Antifungal abilities;Mineral phosphate solubilizing gene

期刊名称：MICROBIOLOGICAL RESEARCH （ 影响因子：5.415； 五年影响因子：6.038 ）

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收录情况： SCI

摘要： Plant growth-promoting rhizobacteria promote plant growth by direct and indirect mechanisms. We isolated twelve bacterial strains showing different degrees of phosphate solubilizing activity from maize rhizosphere. Four isolates solubilized over 300 mu g mL(-1) phosphate from insoluble Ca-3(PO4)2, with isolate SCAUK0330 solubilizing over 450 mu g mL(-1). Based on the 16S rRNA gene sequence analysis SCAUK0330 was identified as Burkholderia cepacia. SCAUK0330 grew at 10-40 degrees C and pH 4.0-10.0, tolerated up to 5% NaCl, and showed antagonism against nine pathogenic fungi. SCAUK0330 promoted the growth of both healthy and Helminthosporium maydis infected maize plants, indicating that the isolate was a good candidate to be applied as a biofertilizer and a biocontrol agent under a wide range of environmental conditions. The expression of a single SCAUK0330 gene gave E. colt a pH decrease linked ability to solubilize phosphate. The nucleotide and the deduced amino acid sequences of this phosphate solubilization linked gene showed high degree of sequence identity with B. cepacia E37gabY. The production of gluconic acid is considered as the principle mechanism for phosphate solubilization. In agreement with the proposed periplasmic location of the gluconic acid production, the predicted signal peptide and transmembrane regions implied that GabY is membrane bound

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