Indian Journal of Science and Technology

Open Access Open Access  Restricted Access Subscription Access

Sequence and Structural Analysis of FtsZ Homologs and Comparison of Bacterial FTsZ with Eukaryotic Tubulins


Affiliations
1 Department of Bioinformatics, Vels University, Pallavaram, Chennai-600117, India
 

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
User

  • Birdsell JA (2002) Integrating genomics, bioinformatics and classical genetics to study the effects of recombination on genome evolution. Mol. Biol. Evol. 19, 1181-1197.

  • Chou PY and Fasman GD (1978) Prediction of the secondary structure of proteins from theiramino acid sequence. Adv.Enzymol.Relat.Areas Mol. Biol. 47, 45-148.

  • Erickson HP, Taylor DW, Taylor KA and Bramhill D (1996) Bacterial cell division protein FtsZ assembles into protofilament sheets and minirings, structural homologs of tubulin polymers. Proc. Natl. Acad. Sci. USA. 93, 519-523.

  • Errington J, Daniel RA and Scheffers DJ (2003) Cytokinesis in bacteria. Microbiol. Mol. Biol. Rev. 67(1), 52-65.

  • Lowe J and Amos LA (1998) Crystal structure of the bacterial cell-division protein FtsZ. Nature. 391, 203-206.

  • Lutkenhaus JF, Wolf-Watz H and Donachie WD (1980) Organization of genes in the ftsA-envA region of the Escherichia coli genetic map and identification of a new fts locus (ftsZ). J. Bacteriol. 142, 615-620.

  • Margolin W, Corbo JC and Long SR (1991) Cloning and characterization of a Rhizobium melliloti homolog of the Escherichia coli cell division gene ftsZ. J. Bacteriol. 173, 5822-5830.

  • Nogales E, Wolf SG and Downing KH (1998) Structure of the αβ tubulin dimer by electron crystallography. Nature. 391, 199-203.

  • Padmalayam I, Anderson B, Kron M, Kelly T and Baumstark B (1997) The 75-Kilodalton antigen of Bartonella bacilliformis is a structural homolog of the cell division protein FtsZ. J. Bacteriol. 179(14), 4545-4552.

  • Schlieper D, Oliva MA, Andreu JM and Löwe J (2005) Structure of bacterial tubulin BtubA/B: Evidence for horizontal gene transfer. PNAS 102 (26), 9170-9175.

  • Singh JK, Makde RD, Kumar V and Panda D (2007) A membrane protein EzrA regulates assembly dynamics of FtsZ by interacting with the C-terminal tail of FtsZ. Biochem. 46(38), 11013-110122.

  • Singh JK, Makde RD, Kumar V and Panda D (2008) SepF increases the assembly and bundling of FtsZ polymers and stabilizes FtsZ protofilaments by binding along its length.http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2662178/ ‐ fn1 J. Biol. Chem. 283(45), 31116–31124

  • Thompson JD, Higgins DG and Gibson TJ (1994) CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22 (22), 4673-4680.

  • Vaughan S, Wickstead B, Gull K and Addinall SG (2004) Molecular evolution of FtsZ protein sequences encoded within the genomes of archaea, bacteria, and eukaryota. J. Mol. Evol. 58, 19–29.

  • Yee B, Lafi FF, Oakley B, Staley JT and Fuerst JA (2007) A canonical FtsZ protein in Verrucomicrobium spinosum, a member of the bacterium phylum Verrucomicrobia that also includes tubulin producing Prosthecobacter species. BMC Evol. Biol. 12 (7), 37.


Abstract Views: 373

PDF Views: 161




  • Sequence and Structural Analysis of FtsZ Homologs and Comparison of Bacterial FTsZ with Eukaryotic Tubulins

Abstract Views: 373  |  PDF Views: 161

Authors

Radha Mahendran
Department of Bioinformatics, Vels University, Pallavaram, Chennai-600117, India
F. Josephine Jenifer
Department of Bioinformatics, Vels University, Pallavaram, Chennai-600117, India
M. Palanimuthu
Department of Bioinformatics, Vels University, Pallavaram, Chennai-600117, India
S. Subasri
Department of Bioinformatics, Vels University, Pallavaram, Chennai-600117, India

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

References





DOI: https://doi.org/10.17485/ijst%2F2011%2Fv4i2%2F29949