Indian Journal of Science and Technology

Abstract

FtsZ, a bacterial cell division protein is a homolog of eukaryotic tubulins. It was postulated that FtsZ of different bacterial species might have specific signature sequences, based on which various FtsZ protein sequences were classified, mined and analyzed. Multiple sequence alignment of the sequences resulted in the highly specific signatures at the C-terminal end of gram-negative bacterial FtsZ. Interestingly, a few organisms belonging to the phylum Bacteroidetes were found to contain 600-650 amino acid-FtsZ sequences having an extra long spacer residues of about 300-350 amino acids. Sequentially, the spacer showed the presence of coils throughout using secondary structure prediction methods. Structurally over a span of 133 residues, a match was found in T7 DNA ligase, suggesting the presence of viral origin of the extra residues. Eukaryotic α-tubulins were also mined and aligned giving rise to high percentage identity even among highly diverged species such as the zebra fish and humans. This suggests the reason behind the high divergence seen between the eukaryotes and the prokaryotes sequentially, though structurally they share 98% similarity. The main focus of the present work was to understand evolution of the bacterial and eukaryotic cytoskeleton proteins.
Keywords: FTsZ, signature sequence, Bacteroidetes, T7 DNA ligase, tubulin, phylogenetic analysis.