Abstract
The DNA sequences of the 14 exon junctions in the murine α-fetoprotein gene were determined using cloned genomic DNA. When these exons were examined with respect to the polypeptide segments they encoded, a direct correspondence between a threefold repeat of four exons and three protein domains was observed. Nucleotide sequence comparisons among the four exons of each domain were used to deduce the likely structure of the primordial domain, and the order and mechanism of its triplication to form the tripartite ancestral gene from which both α-fetoprotein and serum albumin arose. Sequence homologies among the four exons that constitute a single domain also suggest that they were derived, at least in part, from a common sequence which underwent successive amplification and divergence.
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References
Gorin, M. B., Cooper, D. L., Eiferman, F., van de Rijn, P. & Tilghman, S. M. J. biol. Chem. 256, 1954–1959 (1981).
Kioussis, D. et al J. biol. Chem. 256, 1960–1967 (1981).
Jagodzinski, L. L., Sargent, T. D., Yang, M., Glackin, C. & Bonner, J. Proc. natn. Acad. Sci. U.S.A. 78, 3521–3525 (1981).
Liao, W. S. L., Hamilton, R. W. & Taylor, J. M. J. biol. Chem. 255, 8046–8049 (1980).
Innis, M. A. & Miller, D. L. J. biol. Chem. 255, 8994–8996 (1980).
Law, S. W. & Dugaiczyk, A. Nature 291, 201–205 (1981).
D'Eustachio, P., Ingram, R. S., Tilghman, S.M. & Ruddle, F. Somatic Cell Gen. 7, 289–294 (1981).
Ingram, R. S., Scott, R. W. & Tilghman, S. M. Proc. natn. Acad. Sci. U.S.A. 78, 4694–4698 (1981).
Brown, J. R. Fedn Proc. 35, 2141–2144 (1976).
Brown, J. R. Proc. FEBS 11th Meet. 50, 1–10 (1977).
Maxam, A. & Gilbert, W. Proc. natn. Acad. Sci. U.S.A. 74, 560–564 (1977).
Lerner, M. R., Boyle, J. A., Mount, S. M., Wolin, S. L. & Steitz, J. A. Nature 283, 220–224 (1980).
Breathnach, R., Benoist, C., O'Hare, K., Gannon, F. & Chambon, P. Proc. natn. Acad. Sci. U.S.A. 75, 4853–4857 (1978).
Berk, A. & Sharp, P. Cell 12, 721–732 (1977).
Efstratiadis, A. et al. Cell 21, 653–668 (1980).
Baker, C. C. & Ziff, E. B. J. molec. Biol. 149, 189–222 (1981).
Proudfoot, N. J. & Brownlee, G. G. Nature 263, 211–214 (1976).
Fitzgerald, M. & Shenk, T. Cell 24, 251–260 (1981).
Peters, T. & Reed, R. G. Proc. FEBS 11th Meet. 50, 11–20 (1977).
Early, P. W., Davis, M. M., Kaback, D. B., Davidson, N. & Hood, L. Proc. natn. Acad. Sci. U.S.A. 76, 857–861 (1979).
Sakano, H. et al Nature 277, 627–633 (1979).
Gough, N. M., Kemp, D. J., Tyler, B. M., Adams, J. M. & Cory, S. Proc. natn. Acad. Sci. U.S.A. 77, 554–558 (1980).
Calame, K. et al. Nature 284, 452–455 (1980).
Honjo, T. et al. Cell 18, 559–568 (1979).
Dorrington, K. J. Can. J. Biochem. 56, 1087–1101 (1978).
Stein, J. P., Catterall, J. F., Kristo, P., Means, A. R. & O'Malley, B. W. Cell 21, 681–687 (1980).
Gilbert, W. Nature 271, 501 (1978).
Darnell, J. E. Science 202, 1257–1259 (1978).
Tiemeier, D. C. et al. Cell 14, 237–244 (1978).
Lomedico, P. et al. Cell 18, 545–558 (1979).
Gilbert, W. in Eucaryotic Gene Regulation (eds Axel, R., Maniatis, T. & Fox, C. F.) 1-12 (Academic, New York, 1979).
Sippel, A. E., Grez, M. & Schultz, G. Proc. natn. Acad. Sci. U.S.A. 77, 5759–5763 (1980).
Beryajati, C., Place, A. R., Powers, D. A. & Sofer, W. Proc. natn. Acad. Sci. U.S.A. 78, 2717–2721 (1981).
Craik, C. S., Buchman, S. R. & Beychok, S. Proc. natn. Acad. Sci. U.S.A. 77, 1384–1388 (1980).
Craik, C. S., Buchman, S. R. & Beychok, S. Nature 291, 87–90 (1981).
Go, M. Nature 291, 90–92 (1981).
Jensen, E. O., Paludan, K., Neilsen-Hyldig, J. J., Jorgensen, P. & Marker, K.A. Nature 291, 677–679 (1981).
Staden, R. Nucleic Acids Res. 4, 4037–4051 (1977); 5, 1013–1015 (1978).
Queen, C. L. & Korn, L. J. Meth. Enzym. 65, 595–609 (1980).
Sargent, T. D., Yang, M. & Bonner, J. Proc. natn. Acad. Sci. U.S.A. 78, 243–246 (1981).
Sargent, T. D., Jagodzinski, L. L., Yang, M. & Bonner, J. Molec. Cell. Biol. 1, 871–883 (1981).
de Jong, W. W. & Ryden, L. Nature 290, 157–159 (1981).
Nishioka, Y., Leder, A. & Leder, P. Proc. natn. Acad. Sci. U.S.A. 77, 2806–2809 (1980).
Yamada, Y. et al. Cell 22, 887–892 (1980).
McLachlan, A. D. & Walker, J. E. J. molec. Biol. 112, 543–558 (1977).
Gorin, M. B. & Tilghman, S. M. Proc. natn. Acad. Sci. U.S.A. 77, 1351–1355 (1980).
Favaloro, J., Tressman, R. & Kamen, R. Meth. Enzym. 65, 718–749 (1980).
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Eiferman, F., Young, P., Scott, R. et al. Intragenic amplification and divergence in the mouse α-fetoprotein gene. Nature 294, 713–718 (1981). https://doi.org/10.1038/294713a0
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DOI: https://doi.org/10.1038/294713a0
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