The cDNA-Derived Amino Acid Sequence of Hemoglobin I from Lucina pectinata
Tóm tắt
The tropical clam Lucina pectinata contains a unique hemoglobin (HbI) which serves to transport H2S to autotrophic bacteria. The cDNA-derived amino acid sequence was obtained from overlapping clones containing the cDNA that codes for HbI. The reverse transcriptase-polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends (RACE) methods were employed to synthesize the cDNA fragments. An initial 354-bp cDNA clone encoding 118 amino acid residues of HbI was amplified from total RNA by RT-PCR using degenerate oligonucleotides. Gene-specific primers derived from the HbI-partial cDNA sequence were used for obtaining the 5′ and 3′ ends of the cDNA by RACE. The length of the HbI cDNA, estimated from sequence analysis of overlapping clones, was 1322 bp for the full-length cDNA. The coding region of the full-length cDNA codes for 143 amino acid residues. The most conserved amino acid residues in HbI from Lucina pectinata were identified by a multiple alignment with nonvertebrate globin sequences.
Tài liệu tham khảo
Altschul, S. F., Madden, T. L., Schäffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997). Nucleic Acids Res. 25, 3389–3402.
Bolognesi, M., Rosano, C., Losso, R., Borassi, A., Rizzi, M., Wittenberg, J. B., Boffi, A., and Ascenzi, P. (1999). Biophys. J. 77, 1093–1099.
Cerda, J., Echevarría, Y., Morales, E., and López-Garriga, J. (1999). Biospectroscopy 5, 200–213.
Cerda-Colón, J., Silfa, E., and López-Garriga, J. (1998). J. Am. Chem. Soc. 120, 9312–9317.
Chomczynski, P., and Sacchi, N. (1987). Anal. Biochem. 162, 156–159.
Cutruzzolà, F., Travaglini Allocatelli, C., Bracanceio, A., and Brunori, M. (1996). Biochem. J. 314, 83–90.
De Baere, I., Perutz, M. F., Kiger, L., Marden, M. C., and Poyart, C. (1994). Proc. Natl. Acad. Sci. USA 91, 1594–1597.
Dewilde, S., Winnepenninckx, B., Arndt, M. H. L., Nascimento, D. G., Santoro, M., Knight, M., Miller, A. N., Kerlavage, A. R., Geoghagen, N., Van Marck, E., Liu, L. X., Weber, R. E., and Moens, L. (1998). J. Biol. Chem. 273, 13583–13592.
Dikshit, K. L., Orii, Y., Navani, N., Patel, S., Huang, H., Stark, B., and Webster, D. A. (1998). Arch. Biochem. Biophys. 349, 161–166.
Furuta, H., and Kajita, A. (1983). Biochemistry 22, 917–922.
Gambacurta, A., Piro, M. C., and Ascoli, F. (1993). FEBS Lett. 330, 90–94.
Gruhl, M. C., Kao, W. Y., and Bergtrom, G. (1997). J. Mol. Evol. 45, 499–508.
Hockenhull-Johnson, J. D., Stern, M. S., Martin, P., Dass, C., Desiderio, D. M., Wittenberg, J., Vinogradov, S. N., and Walz, D. A. (1991). J. Protein Chem. 10, 609–622.
Hockenhull-Johnson, J. D., Stern, M. S., Wittenberg, J. B., Vinogradov, S. N., Kapp, O. H., and Walz, D. A. (1993). J. Protein Chem. 12, 261–277.
Ishikawa, H. (1977). Comp. Biochem. Physiol. 58, 1–7.
Kitto, G. B., Erwin, D., West, R., and Omnaas, J. (1976). Comp. Biochem. Physiol. B 55, 105–107.
Kitto, G. B., Thomas, P. W., and Hackert, M. L. (1998). J. Exp. Zool. 282, 120–126.
Kraus, D. W., and Wittenberg, J. B. (1990). J. Biol. Chem. 265, 16043–16053.
Kraus, D. W., Wittenberg, J. B., Jing-Fen, L., and Peisach, J. (1990). J. Biol. Chem. 265, 16054–16059.
Navarro, A. M., Maldonado, M., González-Lagoa, J., López-Mejía, R., López-Garriga, J., and Colón, J. (1996). Inorg. Chim. Acta 243, 161–166.
Nguyen, B. D., Zhao, X., Vyas, K., La Mar, G. N., Lile, R. A., Brucker, E. A., Phillips, G. N. Jr., Olson, J. S., and Witterberg, J. B. (1998). J. Biol. Chem. 273, 9517–9526.
Read, K. R. H. (1962). Biol. Bull. 123, 605–617.
Rizzi, M., Wittenberg, J. B., Coda, A., Fasano, M., Ascenzi, P., and Bolognesi, M. (1994). J. Mol. Biol. 244, 86–99.
Rizzi, M., Wittenberg, J. B., Coda, A., Ascenzi, P., and Bolognesi, M. (1996). J. Mol. Biol. 258, 1–5.
Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989). Molecular Cloning: A Laboratory Manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, New York, pp. 1–3.
Sanoguet, Z., and López-Garriga, J. (n.d.). Manuscript in preparation.
Silfa, E., Almeida, M., Cerda, J., Wu, S., and López-Garriga, J. (1998). Biospectroscopy 4, 311–326.
Spencer, N. (1984). J. Mol. Biol. 107, 405–415.
Suzuki, T. (1986). J. Biol. Chem. 261, 3692–3699.
Suzuki T., and Furukohri, T. (1990). J. Protein Chem. 9, 69–73.
Suzuki, T., Takagi, T., and Ohta, S. (1989a). Biochem. J. 260, 177–182.
Suzuki, T., Takagi, T., and Ohta, S. (1989b). Biochim. Biophys. Acta 999, 254–259.
Takano, T. (1977). J. Mol. Biol. 110, 537–568.
Wakabayashi, S., Matsubara, H., and Webster, D. A. (1986). Nature 322, 481–483.
Wittenberg, J. B., and Kraus, D. W. (1991). Hemoglobins of eukaryote/prokaryote symbioses. In Structure and Function of Invertebrate Oxygen Carriers (Vinogradov, S. N., and Kapp, O. H., Eds.), Springer, New York, pp. 323–329.