Ocean Science Journal

The Korean Society of Oceanography (한국해양학회)
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Nucleotide Sequence of ${\beta}-tubulin$ Gene from the Soft Coral Scleronephthya gracillimum $(K\ddot{u}kenthal)$

  • Yum, Seung-Shic (Southern Coastal Environment Research Division, South Sea Institute, KORDI) ;
  • Woo, Seon-Ock (Southern Coastal Environment Research Division, South Sea Institute, KORDI) ;
  • Chang, Man (Southern Coastal Environment Research Division, South Sea Institute, KORDI) ;
  • Lee, Taek-Kyun (Southern Coastal Environment Research Division, South Sea Institute, KORDI) ;
  • Song, Jun-Im (Department of Biological Science, College of Natural Sciences, Ewha Womans University)
  • Published : 2005.03.31
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Abstract

We cloned the complete cDNA of the ${\beta}-bubulin$ from the soft coral, Scleronephthya gracillimum $(K\ddot{u}kenthal)$ (Alcyonacea, Octocorallia, Anthozoa, Cnidaria), via the random sequencing of a cDNA library and the 5'-rapid amplification of cDNA end (RACE) technique. The full-length cDNA of the S. gracillimum ${\beta}-tubulin$ comprised 1541 bp, not including the poly $A^+$ stretch, also contained a complete open reading frame, which codes for a total of 445 amino acids. The amino acid residues 16402 appeared to be in a state of conservation in a variety of animals. Northern blot analysis clearly demonstrated that the sequence we have obtained is, indeed, the full-length cDNA of the ${\beta}-bubulin$ gene in S. gracillimum.

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References

  1. Amos, L.A., F. van den Ent, and J. Lowe. 2004. Structural/functional homology between the bacterial and eukaryotic cytoskeletons. Curr. Opin. Cell Biol., 16, 24-31 https://doi.org/10.1016/j.ceb.2003.11.005
  2. Aniello, F., D. Couchie, D. Gripois, and J. Nunez. 1991. Regulation of five tubulin isotypes by thyroid hormone during brain development. J. Neurochem., 57, 1781-1786 https://doi.org/10.1111/j.1471-4159.1991.tb06381.x
  3. Baumann, P. and S.P. Jackson. 1996. An archaebacterial homologue of the essential eubacterial cell division protein FtsZ. Proc. Natl. Acad. Sci. U.S.A., 93, 6726-6730
  4. Bieker, J.J. and M. Yazdani-Buicky. 1992. The multiple betatubulin genes of Xenopus: isolation and developmental expression of a germ-cell isotype beta-tubulin gene. Differentiation, 50, 15-23 https://doi.org/10.1111/j.1432-0436.1992.tb00481.x
  5. Burgoyne, R.D., M.A. Cambray-Deakin, S.A. Lewis, S. Sarkar, and N.J. Cowan. 1988. Differential distribution of betatubulin isotypes in cerebellum. Embo. J., 7, 2311-2319
  6. de Boer, P., R. Crossley, and L. Rothfield. 1992. The essential bacterial cell-division protein FtsZ is a GTPase. Nature, 359, 254-256 https://doi.org/10.1038/359254a0
  7. Erickson, H.P. 1998. Atomic structures of tubulin and FtsZ. Trends Cell Biol., 8, 133-7 https://doi.org/10.1016/S0962-8924(98)01237-9
  8. Erickson, H.P. and E.T. O'Brien. 1992. Microtubule dynamic instability and GTP hydrolysis. Annu. Rev. Biophys. Biomol. Struct., 21, 145-166 https://doi.org/10.1146/annurev.bb.21.060192.001045
  9. Gupta, M.L., Jr., C.J. Bode, C.A. Dougherty, R.T. Marquez, and R.H. Himes. 2001. Mutagenesis of beta-tubulin cysteine residues in Saccharomyces cerevisiae: mutation of cysteine 354 results in cold-stable microtubules. Cell Motil. Cytoskeleton, 49, 67-77 https://doi.org/10.1002/cm.1021
  10. Gupta, M.L., Jr., C.J. Bode, D.A. Thrower, C.G. Pearson, K.A. Suprenant, K.S. Bloom, and R.H. Himes. 2002. beta-Tubulin C354 mutations that severely decrease microtubule dynamics do not prevent nuclear migration in yeast. Mol. Biol. Cell, 13, 2919-2932 https://doi.org/10.1091/mbc.E02-01-0003
  11. Hall, J.L., L. Dudley, P.R. Dobner, S.A. Lewis, and N.J. Cowan. 1983. Identification of two human beta-tubulin isotypes. Mol. Cell Biol., 3, 854-862 https://doi.org/10.1128/MCB.3.5.854
  12. Joshi, H.C. and D.W. Cleveland. 1989. Differential utilization of beta-tubulin isotypes in differentiating neurites. J. Cell Biol., 109, 663-673 https://doi.org/10.1083/jcb.109.2.663
  13. Lewis, S.A., M.G. Lee, and N.J. Cowan. 1985. Five mouse tubulin isotypes and their regulated expression during development. J. Cell Biol., 101, 852-861 https://doi.org/10.1083/jcb.101.3.852
  14. Margolin, W., R. Wang, and M. Kumar. 1996. Isolation of an FtsZ homolog from the archaebacterium Halobacterium salinarium: implications for the evolution of FtsZ and tubulin. J. Bacteriol., 178, 1320-1327 https://doi.org/10.1128/jb.178.5.1320-1327.1996
  15. Mejillano, M.R., B.D. Shivanna, and R.H. Himes. 1996. Studies on the nocodazole-induced GTPase activity of tubulin. Arch. Biochem. Biophys., 336, 130-138 https://doi.org/10.1006/abbi.1996.0540
  16. Mitchison, T. and M. Kirschner. 1984. Dynamic instability of microtubule growth. Nature, 312, 237-242 https://doi.org/10.1038/312237a0
  17. RayChaudhuri, D. and J.T. Park. 1992. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature, 359, 251-254 https://doi.org/10.1038/359251a0
  18. van den Ent, F., L. Amos, and J. Lowe. 2001. Bacterial ancestry of actin and tubulin. Curr. Opin. Microbiol., 4, 634-638 https://doi.org/10.1016/S1369-5274(01)00262-4
  19. Woo, S., M. Yoon, D.-S. Suh, J.-I. Song, J.H. Kim, and S. Yum. 2004. Molecular cloning of the translation elongation factor 1A (eEF1A) gene from the soft coral, Scleronephthya gracillimum (Kukenthal) and implication on cnidarian phylogeny. Korean J. Genetics, 26, 387-395
  20. Wright, A.J. and C.P. Hunter. 2003. Mutations in a beta-tubulin disrupt spindle orientation and microtubule dynamics in the early Caenorhabditis elegans embryo. Mol. Biol. Cell, 14, 4512-4525 https://doi.org/10.1091/mbc.E03-01-0017
  21. Yoshikawa, M., G. Yang, K. Kawaguchi, and S. Komatsu. 2003. Expression analyses of beta-tubulin isotype genes in rice. Plant Cell Physiol., 44, 1202-1207 https://doi.org/10.1093/pcp/pcg150