Journal of Pure and Applied MicrobiologyVol. 9 No. 2

Comparative Analysis of 1-aminocyclopropane-1-carboxylate (ACC) Deaminase in Selected Plant Growth Promoting Rhizobacteria (PGPR)

Satendra Singh1, Sudha Kumari Yadav1, Pallavi Mishra1, Ranjeet Maurya1, Viswanath Rana1, Arvind Kumar Yadav1, Anamika Singh2, Gurudayal Ram3 and Pramod W. Ramteke4

1Department of Computational Biology & Bioinformatics, SHIATS, Allahabad - 211007, India. 2Department of Botany, Maitreyi College, University of Delhi, India. 3Department of Tissue Engineering, JSBB, SHIATS, Allahabad - 211007, India. 4 Department of Biological Sciences, SHIATS, Allahabad - 211007, India.

Received on 16 April 2015 and accepted on 06 May 2015



1-aminocyclopropane-1-carboxylate (ACC) deaminase promotes plant growth by sequestering and cleaving the ethylene precursor ACC to a-ketobutyrate and ammonium. Many plant growth promoting rhizobacteria producing 1-aminocyclopropane-1-carboxylate (ACC) deaminase as a source of nitrogen has an eminent role in plant nutrition. In this work to perform comparative proteomics analysis of ACCD producing plant growth-promoting rhizobacteria (PGPR) i.e., Azospirillum lipoferum, Phyllobacterium brassicacearum, Pseudomonas fluorescens, Francisella tularensis subsp. holarctica OSU18 and Bacillus cereus. The sequence and phylogenetic analysis of ACCD producing PGPR species represents the common conserved domain belonging to the tryptophan synthase beta subunit-like PLP-dependent enzymes superfamily and closely related to each other. The predicted homology models of ACCD of PGPR have similar protein structure with similar folds often share similar function. This analysis represents the evolutionary conservation and same biochemical function of ACCD producing plant growth-promoting rhizobacteria.

Keywords : ACCD, PGPR, a-ketobutyrate, Ammonium, Proteome, Evolutionary conservation.