Genome level analysis of bacteriocins of lactic acid bacteria. (June 2015)

• Record Type: Journal Article
• Authors: Singh, Neetigyata Pratap; Tiwari, Abhay; Bansal, Ankiti; Thakur, Shruti; Sharma, Garima; Gabrani, Reema
• Is Part Of: Computational biology and chemistry. Volume 56(2015)
• Page Start: 1
• Page End: 6
• Publication Date: 2015-06
• Subjects: Bacteriocins -- BAGEL3 -- MEGA6 -- ProtParam -- SOPMA; Chemistry -- Data processing -- Periodicals; Biology -- Data processing -- Periodicals; Biochemistry -- Data processing; Biology -- Data processing; Molecular biology -- Data processing; Periodicals; Electronic journals; 542.85
• DOI: 10.1016/j.compbiolchem.2015.02.013
• Languages: English
• ISSNs: 1476-9271

Abstract

Graphical abstract: Highlights: Identification of bacteriocin secretors lactic acid bacteria and biosynthetic gene with bioinformatic tools. Phylogenetic tree of LAB with 16S rRNA, rpoB and gyrB (housekeeping genes) by MEGA6 tool. Physiochemical and secondary structure analysis of putative strains by computational methodology. Abstract: Bacteriocins are antimicrobial peptides which are ribosomally synthesized by mainly all bacterial species. LABs (lactic acid bacteria) are a diverse group of bacteria that include around 20 genera of various species. Though LABs have a tremendous potential for production of anti-microbial peptides, this group of bacteria is still underexplored for bacteriocins. To study the diversity among bacteriocin encoding clusters and the putative bacteriocin precursors, genome mining was performed on 20 different species of LAB not reported to be bacteriocin producers. The phylogenetic tree of gyrB, rpoB, and 16S rRNA were constructed using MEGA6 software to analyze the diversity among strains. Putative bacteriocins operons identified were found to be diverse and were further characterized on the basis of physiochemical properties and the secondary structure. The presence of at least two cysteine residues in most of the observed putative bacteriocins leads to disulphide bond formation and provide stability. Our data suggests that LABs are prolific source of low molecular weight non modified peptides.