16
Views
5
CrossRef citations to date
0
Altmetric
Original Article

Genomic Cloning of a Heat Shock Cognate 71-1 Gene (HSC71-1) from the Hermaphroditic Fish Rivulus marmoratus (Cyprinodontiformes, Rivulidae)

Pages 33-38 | Received 13 Aug 2003, Published online: 11 Jul 2009

References

  • Arai, A., Naruse, K., Mitani, H. and Shima, A. (1995) “Cloning and characterization of cDNAs for 70-kDa heat-shock proteins (Hsp70) from two fish species of the genus Oryzias”, Jpn. J. Genet. 70, 423– 433.
  • Basu, N., Todgham, A.E., Ackerman, P.A., Bibeau, M.R., Nakano, K., Schulte, P.M. and Iwama, G.K. (2002) “Heat shock protein genes and their functional significance in fish”, Gene 295, 173– 183.
  • Boone, A.N. and Vijayan, M.M. (2002) “Constitutive heat shock protein 70 (HSC70) expression in rainbow trout hepatocytes: effect of heat shock and heavy metal exposure”, Comp. Biochem. Physiol. 132C, 223– 233.
  • DiIorio, P.J., Holsinger, K., Schultz, R.J. and Hightower, L.E. (1996) “Quantitative evidence that both Hsc70 and Hsp70 contribute to thermal adaptation in hybrids of the livebearing fishes Poeciliopsis”, Cell Stress Chaperones 1, 139– 147.
  • Felsenstein, J. (1996) “Inferring phylogeny from protein sequences by parsimony, distance, and likelihood methods”, Methods Enzymol. 266, 368– 382.
  • Graser, R.T., Malnar-Dragojevic, D. and Vincek, V. (1996) “Cloning and characterization of a 70 kd heat shock cognate (hsc70) gene from the zebrafish (Danio rerio)”, Genetica 98, 273– 276.
  • Lee, J.-S., Choe, J. and Park, E.-H. (1995) “Genomic structure of c-Ki-ras proto-oncogene of the hermaphroditic fish Rivulus mamoratus (Teleostei: Rivulidae)”, Biochem. Mol. Biol. Int. 35, 57– 63.
  • Lele, Z., Engel, S. and Krone, P.H. (1997) “hsp47 and hsp70 gene expression is differentially regulated in a stress- and tissue- specific manner in zebrafish embryos”, Dev. Genet. 21, 123– 133.
  • Molina, A., Di Martino, E., Martial, J.A. and Muller, M. (2001) “Heat shock stimulation of a tilapia heat shock protein 70 promoter is mediated by a distal element”, Biochem. J. 356, 353– 359.
  • Page, R.D.M. (1996) “TreeView: an application to display phylogenetic trees on personal computers”, Comput. Appl. Biol. Sci. 12, 357– 358.
  • Park, J.-H., Lee, J.J., Yoon, S., Lee, J.-S., Choe, S.Y., Choe, J., Park, E.-H. and Kim, C.G. (2001) “Genomic cloning of the Hsc71 gene in the hermaphroditic teleost Rivulus marmoratus and analysis of its expression in skeletal muscle: identification of a novel muscle-preferred regulatory element”, Nucleic Acids Res. 29, 3041– 3050.
  • Place, S.P. and Hofmann, G.E. (2001) “Temperature interactions of the molecular chaperone Hsc70 from the eurythermal marine goby Gillichthys mirabilis”, J. Exp. Biol. 204, 2675– 2682.
  • Said Ali, K., Dorgai, L., Abraham, M. and Hermesz, E. (2003) “Tissue- and stressor-specific differential expression of two hsc70 genes in carp”, Biochem. Biophys. Res. Commun. 307, 503– 509.
  • Santacruz, H., Vriz, S. and Angelier, N. (1997) “Molecular characterization of a heat shock cognate cDNA of zebrafish, hsc70, and developmental expression of the corresponding transcripts”, Dev. Genet. 21, 223– 233.
  • Tawk, M., Joulie, C. and Vriz, S. (2000) “Zebrafish Hsp40 and Hsc70 genes are both induced during caudal fin regeneration”, Mech. Dev. 99, 183– 186.
  • Thompson, J.D., Higgins, D.G. and Gibson, T.J. (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, 4673– 4680.
  • Yokoyama, Y., Hashimoto, H., Kubota, S., Kinoshita, M., Toyohara, H., Sakaguchi, M., Tanaka, M., Seikai, T. and Kanamori, M. (1998) “cDNA cloning of heat-inducible HSP70, a 70.6 kDa heat shock protein, in Japanese flounder Paralichtys olivaceus”, Fisheries Sci. 64, 964– 968.
  • Zafarullah, M., Wisniewski, J., Shworak, N.W., Schieman, S., Misra, S. and Gedamu, L. (1992) “Molecular cloning and characterization of a constitutively expressed heat-shock- cognate hsc71 gene from rainbow trout”, Eur. J. Biochem. 204, 893– 900.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.