Abstract
The tetrameric haemoglobins of vertebrates are encoded by α-and β-globin gene families which arose during evolution by a succession of gene duplications, commencing with an αβ globin gene duplication which occurred about 500 Myr ago, early in the evolution of the vertebrates1,3. All functional α- and β-globin genes analysed so far share common features, including coding sequence homologies and the presence of two introns within the coding sequence at locations which correlate with interdomain boundaries within globin polypeptides4–7. Here we describe the isolation and characterization of an additional diverged member of the globin gene family, the seal myoglobin gene. We show that monomeric myoglobin, which diverged from haemoglobin about 600–800 Myr ago before the appearance of tetrameric haemoglobins8,9, is also specified by a gene containing two introns at positions precisely homologous to haemoglobin introns. Unlike vertebrate haemoglobin genes, however, the noncoding regions of the seal myoglobin gene are remarkably long.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on SpringerLink
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Dayhoff, M. O. (ed.) Atlas of Protein Sequence and Structure Vol. 5 (Natn. Biomed. Res. Foundation, Silver Spring, Maryland, 1972).
Efstratiadis, A. et al. Cell 21, 653–668 (1980).
Jeffreys, A.J. in Genome Evolution (eds Dover, G. A. & Flavell, R. B.) 157–176 (Academic, London, 1982).
Craik, C. S., Buchman, S. R. & Beychok, S. Proc. natn. Acad. Sci. U.S.A. 77, 1384–1388 (1980).
Eaton, W. A. Nature 284, 183–185 (1980).
Craik, C. S., Buchman, S. R. & Beychok, S. Nature 291, 87–90 (1981).
Gō, M. Nature 291, 90–92 (1981).
Hunt, T. L., Hurst-Calderone, S. & Dayhoff, M. O. in Atlas of Protein Sequence and Structure (ed. Dayhoff, M. O.) 229–251 (Natn. Biomed. Res. Foundation, Washington DC, 1978).
Czelusniak, J. et al. Nature 15, 297–300 (1982).
Slijper, E. J. Whales (Hutchinson, London, 1962).
Hempleman, H. V. & Lockwood, A. P. M. The Physiology of Diving in Man and Other Animals (Edward Arnold, London, 1978).
Wood, D., Blanchetot, A. & Jeffreys, A.J. 10, 7133–7144 (1982).
Loenen, W. A. M. & Brammar, W. J. Gene 20, 249–259 (1980).
Twigg, A. J. & Sherratt, D. Nature 283, 216–218 (1980).
Bradshaw, R. A. & Gurd, F. R. N. J. biol. Chem. 244, 2167–2181 (1969).
Weaver, R. F. & Weissmann, C. Nucleic Acids Res. 7, 1175–1193 (1979).
Breathnach, R. & Chambon, P. A. Rev. Biochem. 50, 349–383 (1981).
Jensen, E. O., Paludan, K., Hyldig-Nielsen, J. J., Jørgensen, P. & Marcker, K. A. Nature 291, 677–679 (1981).
Brisson, N. & Verna, D. P. S. Proc. natn. Acad. Sci. U.S.A. 79, 4055–4059 (1982).
Wiborg, O., Hyldig-Nielsen, J. J., Jensen, E. ø., Paludan, K. & Marcker, K. A. Nucleic Acids Res. 10, 3487–3494 (1982).
Hyldig-Nielsen, J. J. et al. Nucleic Acids Res. 10, 689–701 (1982).
Gilbert, W. Nature 271, 501 (1978).
Darnell, J. E. Science 202, 1257–1260 (1978).
Blake, C. C. F. Nature 277, 598 (1979).
Reanney, D. Nature 277, 598–600 (1979).
Van Den Berg, J. et al. Nature 276, 37–44 (1978).
Liebhaber, S. A., Goossens, M. J. & Kan, Y. W. Proc. natn. Acad. Sci. U.S.A. 77, 7054–7058 (1980).
Nishioka, Y. & Leder, P. Cell 18, 875–882 (1979).
Schon, E. A., Wernke, S. M. & Lingrel, J. B. J. biol. Chem. 257, 6825–6835 (1982).
Lawn, R. M., Efstratiadis, A., O'Connell, C. & Maniatis, T. Cell 21, 647–651 (1980).
Spritz, R. A., DeRiel, J. K., Forget, B. G. & Weissmann, S. M. Cell 21, 639–646 (1980).
Slightom, J. L., Blechl, A. E. & Smithies, O. Cell 21, 627–638 (1980).
Baralle, F. E., Shoulders, C. C. & Proudfoot, N. J. Cell 21, 621–626 (1980).
Konkel, D. A., Maizel, J. V. & Leder, P. Cell 18, 865–873 (1979).
Van Ooyen, A., Van Den Berg, J., Mantei, N. & Weissmann, C. Science 206, 337–344 (1979).
Haynes, J. R., Rosteck, P. J. R. & Lingrel, J. B. Proc. natn. Acad. Sci. U.S.A. 77, 7127–7131 (1980).
Schon, E. A., Cleary, M. L., Haynes, J. R. & Lingrel, J. B. Cell 27, 359–369 (1981).
Jeffreys, A. J. et al. J. molec. Biol. 156, 487–503 (1982).
Chaconas, G. & Van de Sande, J. H. Meth. Enzym. 65, 75–85 (1980).
Maxam, A. M. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Blanchetot, A., Wilson, V., Wood, D. et al. The seal myoglobin gene: an unusually long globin gene. Nature 301, 732–734 (1983). https://doi.org/10.1038/301732a0
Received:
Accepted:
Issue date:
DOI: https://doi.org/10.1038/301732a0
This article is cited by
-
Evolutionary history of introns in a multidomain globin gene
Journal of Molecular Evolution (1996)
-
Evolution of a polymeric globin in the brine shrimp Artemia
Nature (1990)
-
Primary structure and promoter analysis of leghemoglobin genes of the stem-nodulated tropical legume Sesbania rostrata: Conserved coding sequences, cis-elements and trans-acting factors
Molecular and General Genetics MGG (1988)
-
Polyadenylation of Chinese hamster dihydrofolate reductase genomic genes and minigenes after gene transfer
Somatic Cell and Molecular Genetics (1987)
