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Issue No:2 Vol.4 |
February -2011 |
ISSN: 0974-5645 |
| RESEARCH ARTICLES |
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| 14. Sequence and structural analysis of FtsZ homologs and comparison of bacterial FTsZ with eukaryotic tubulins. Radha Mahendran, F. Josephine Jenifer, M. Palanimuthu and S. Subasri. Indian J.Sci.Technol. Vol.4, Issue 2, pp: 141-146. |
 
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- 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 resence 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 -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.
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