- 1) Sverdrup, H. U., The Pacific Ocean. Science, New Series, 94, 287–293 (1941).
- 2) Niering, W. A., Terrestrial ecology of Kapingamarangi Atoll, Caroline islands. Ecol. Monogr., 33, 131–160 (1963).
- 3) Weins, H. J., The geography of Kapingamarangi Atoll in the eastern Carolines. Atoll Res. Bull., 48, 1–86 (1956).
- 4) Young, J. C., Agashe, V. R., Siegers, K., and Hartl, F. U., Pathways of chaperone-mediated protein folding in the cytosol. Nat. Rev. Mol. Cell Biol., 5, 781–791 (2004).
- 5) Weibezahn, J., Schlieker, C., Tessarz, P., Mogk, A., and Bukau, B., Novel insights into the mechanism of chaperone-assisted protein disaggregation. Biol. Chem., 386, 739–744 (2005).
- 6) Suutari, M., and Laakso, S., Microbial fatty acids and thermal adaptation. Crit. Rev. Microbiol., 20, 285–328 (1994).
- 7) Lakin-Thomas, P. L., Brody, S., and Cote, G. G., Temperature compensation and membrane composition in Neurospora crassa. Chronobiol. Int., 14, 445–454 (1997).
- 8) Orlowski, J., and Grinstein, S., Na+/H+ Exchangers of mammalian cells. J. Biol. Chem., 272, 22373–22376 (1997).
- 9) Serrano, R., and Rodriguez-Navarro, A., Ion homeostasis during salt stress in plants. Curr. Opin. Cell Biol., 13, 399–404 (2001).
- 10) Hiraide, M., Sunagawa, M., Matsumoto, A., Ono, K., Miyazaki, Y., Fujimoto, K., Lihpai, S., and Tabuchi, R., Census of wood-rotting fungi in mangrove forest on Pohnpei Island, Micronesia: evaluation of the carbon fixation and organic matter decomposition functions in natural mangrove forests, Final Report of Study Supported by Grant-In-Aid for Scientific Research (A)(2) Japan Society for Promotion of Science, pp. 95–105 (2006).
- 11) Sambrook, J., and Russell, D. W., “Molecular Cloning, a Laboratory Manual” Third ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor (2001).
- 12) Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J., Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res., 25, 3389–3402 (1997).
- 13) Saitou, N., and Nei, M., The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Evol. Biol., 4, 406–425 (1987).
- 14) Holden, D. W., Kronstad, J. W., and Leong, S. A., Mutation in a heat-regulated hsp70 gene of Ustilago maydis. EMBO J., 8, 1927–1934 (1989).
- 15) Woodroffe, C. D., and Grindrod, J., Mangrove biogeography: the role of quaternary environmental and sea-level change. J. Biogeogr., 18, 479–492 (1991).
- 16) Saba, J. D., Nara, F., Bielawska, A., Garrett, S., and Hannun, Y. A., The BST1 gene of Saccharomyces cerevisiae is the sphingosine-1-phosphate lyase. J. Biol. Chem., 272, 26087–26090 (1997).
- 17) Zhou, J., and Saba, J. D., Identification of the first mammalian sphingosine phosphate lyase gene and its functional expression in yeast. Biochem. Biophys. Res. Commun., 242, 502–507 (1998).
- 18) Mendel, J., Heinecke, K., Fyrst, H., and Saba, J. D., Sphingosine phosphate lyase expression is essential for normal development in Caenorhabditis elegans. J. Biol. Chem., 278, 22341–22349 (2003).
- 19) Terzaghi, A., Tettamanti, G., and Masserini, M., Interaction of glycosphingolipids and glycoproteins: thermotropic properties of model membranes containing GM1 ganglioside and glycophorin. Biochemistry, 32, 9722–9725 (1993).
- 20) Roth, Z., and Hansen, P. J., Sphingosine 1-phosphate protects bovine oocytes from heat shock during maturation. Biol. Reprod., 71, 2072–2078 (2004).
- 21) Aaronson, L. R., and Martin, C. E., Temperature-induced modifications of glycosphingolipids in plasma membranes of Neurospora crassa. Biochim. Biophys. Acta, 735, 252–258 (1983).
- 22) Sakai, H., and Kajiwara, S., Membrane lipid profile of an edible basidiomycete Lentinula edodes during growth and cell differentiation. Lipids, 39, 67–73 (2004).
- 23) Miyazaki, Y., Nakamura, M., and Babasaki, K., Molecular cloning of developmentally specific genes by representational difference analysis during the fruiting body formation in the basidiomycete Lentinula edodes. Fungal Genet. Biol., 42, 493–505 (2005).
- 24) Kinclova, O., Ramos, J., Potier, S., and Sychrova, H., Functional study of the Saccharomyces cerevisiae Nha1p C-terminus. Mol. Microbiol., 40, 656–668 (2001).
- 25) Waditee, R., Hibino, T., Nakamura, T., Incharoensakdi, A., and Takabe, T., Overexpression of a Na+/H+ antiporter confers salt tolerance on a freshwater cyanobacterium, making it capable of growth in sea water. Proc. Natl. Acad. Sci. USA, 99, 4109–4114 (2002).
- 26) Kis-Papo, T., Oren, A., Wasser, S. P., and Nevo, E., Survival of filamentous fungi in hypersaline Dead Sea water. Microb. Ecol., 45, 183–190 (2003).
- 27) Domanico, S. Z., DeNagel, D. C., Dahlseid, J. N., Green, J. M., and Pierce, S. K., Cloning of the gene encoding peptide-binding protein 74 shows that it is a new member of the heat shock protein 70 family. Mol. Cell. Biol., 13, 3598–3610 (1993).
- 28) Kim, H., Melen, K., Osterberg, M., and von Heijne, G., A global topology map of the Saccharomyces cerevisiae membrane proteome. Proc. Natl. Acad. Sci. USA, 103, 11142–11147 (2006).
Full access
Molecular Cloning of Functional Genes for High Growth-Temperature and Salt Tolerance of the Basidiomycete Fomitopsis pinicola Isolated in a Mangrove Forest in Micronesia
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.
Related research
People also read lists articles that other readers of this article have read.
Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.
Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.