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Journal Article| Volume 267, ISSUE 9, P6147-6157, March 25, 1992

Mutations away from splice site recognition sequences might cis-modulate alternative splicing of goat alpha s1-casein transcripts. Structural organization of the relevant gene.

Open AccessPublished:March 25, 1992DOI:https://doi.org/10.1016/S0021-9258(18)42674-9
Mutations away from splice site recognition sequences might cis-modulate alternative splicing of goat alpha s1-casein transcripts. Structural organization of the relevant gene.
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      alpha s1-Casein variants F and D, synthesized in goat milk at lower levels than variant A, essentially differ from it by internal deletions of 37 and 11 amino acid residues, respectively. Northern blot analysis of mRNAs encoding alpha s1-casein F and A and sequencing of the relevant cloned cDNAs, as well as sequencing of in vitro amplified genomic fragments, revealed multiple alternatively processed transcripts, from the F allele. Although correctly spliced messengers were identified, most of the FmRNAs lacked three exons. These exons, further identified as exons 9, 10, and 11, together encode the 37 amino acid residues present in alpha s1-casein variant A but missing in variant F. Exon 9 codes for the sequence present in variant A but deleted in variant D. A single nucleotide deletion in exon 9 and two insertions, 11 and 3 base pairs in length, in the downstream intron, were identified as mutations potentially responsible for the alternative skipping of these 3 exons. From a computer-predicted secondary structure it appeared that the 11-base pair insertion might be involved in base-pairing interactions with the intron 5' splice site which might consequently be less accessible to U1 snRNA. We also report here the complete structural organization of the goat alpha s1-casein transcription unit, deduced from polymerase chain reaction experiments. It contains 19 exons scattered within a nucleotide stretch nearly 17-kilobase pairs long.

      References

        • Swaisgood H.E.
        Fox P.F. Developments in Dairy Chemistry, 1: Protein. I. Applied Science Publishers, London1982: 1-59
        • Grosclaude F.
        • Mahé M.-F.
        • Brignon G.
        • Di Stasio L.
        • Jeunet R.
        Genet. Select. Evol. 1987; 19: 399-412
        • Mahé M.-F.
        • Grosclaude F.
        Genet. Select. Evol. 1989; 21: 127-129
        • Leroux C.
        • Martin P.
        • Mahé M.-F.
        • Levéziel H.
        • Mercier J.-C.
        Anim. Genet. 1990; 21: 341-351
        • Brignon G.
        • Mahé M.-F.
        • Grosclaude F.
        • Ribadeau Dumas B.
        Protein Sequences Data Anal. 1989; 2: 181-188
        • Brignon G.
        • Mahé M.-F.
        • Ribadeau Dumas B.
        • Mercier J.-C.
        • Grosclaude F.
        Eur. J. Biochem. 1990; 193: 237-241
        • Jones W.K.
        • Yu-Lee L.-Y.
        • Clift S.M.
        • Brown T.L.
        • Rosen J.M.
        J. Biol. Chem. 1985; 260: 7042-7050
        • Bonsing J.
        • Ring J.M.
        • Stewart A.F.
        • MacKinlay A.G.
        Aust. J. Biol. Sci. 1988; 41: 527-537
        • Hobbs A.A.
        • Rosen J.M.
        Nucleic Acids Res. 1982; 10: 8079-8098
        • Cathala G.
        • Savouret J.F.
        • Mendez B.
        • West B.L.
        • Karin M.
        • Martial J.A.
        • Baxter J.D.
        DNA. 1983; 2: 329-335
        • Aviv H.
        • Leder P.
        Proc. Natl. Acad. Sci. U. S. A. 1972; 69: 1408-1412
        • MacMaster G.K.
        • Carmichael G.G.
        Proc. Natl. Acad. Sci. U. S. A. 1977; 74: 4835-4838
        • Mercier J.-C.
        • Gaye P.
        • Soulier S.
        • Hue-Delahaie D.
        • Vilotte J.-L.
        Biochimie. 1985; 67: 959-971
        • Feinberg A.P.
        • Vogelstein B.
        Anal. Biochem. 1984; 137: 266-267
        • Gubler U.
        • Hoffman B.J.
        Gene (Amst.). 1983; 25: 263-269
        • Saiki R.K.
        • Gelfand D.H.
        • Stoffel S.
        • Scharf S.J.
        • Higuchi R.
        • Horn G.T.
        • Mullis K.B.
        • Erlich H.A.
        Science. 1988; 239: 487-491
        • Southern E.M.
        J. Mol. Biol. 1975; 98: 503-517
        • Sanger F.
        • Nicklen S.
        • Coulson A.R.
        Proc. Natl. Acad. Sci. U. S. A. 1977; 74: 5463-5467
        • Hattori M.
        • Sakaki Y.
        Anal. Biochem. 1986; 152: 232-238
        • Stewart A.F.
        • Willis I.M.
        • Mackinlay A.G.
        Nucleic Acids Res. 1984; 12: 3895-3907
        • Erster S.H.
        • Finn L.A.
        • Frendewey D.A.
        • Helfman D.M.
        Nucleic Acids Res. 1988; 16: 5999-6014
        • Gaye P.
        • Gautron J.-P.
        • Mercier J.-C.
        • Haze G.
        Biochem. Biophys. Res. Commun. 1977; 79: 903-911
        • Rosen J.M.
        Neville M.C. Daniel C.W. The Mammary Gland. Plenum Publishing Corp, New York1987: 301-322
        • Mercier J.-C.
        • Vilotte J.-L.
        • Provot C.
        Gelderman H. Ellendorff F. Genome Analysis in Domestic Animals. Verlag VCH, Weinheim, Federal Republic of Germany1990: 233-258
        • Yu-Lee L.-Y.
        • Richter-Mann L.
        • Couch C.H.
        • Stewart A.F.
        • MacKinlay A.G.
        • Rosen J.M.
        Nucleic Acids Res. 1986; 14: 1883-1902
        • Sharp P.A.
        Cell. 1981; 23: 643-646
        • McKnight R.A.
        • Jimenez-Flores R.
        • Kang Y.
        • Creamer L.K.
        • Richardson T.
        J. Dairy Sci. 1989; 72: 2464-2473
        • Mercier J.-C.
        • Grosclaude F.
        • Ribadeau Dumas B.
        Eur. J. Biochem. 1971; 23: 41-51
        • Green M.R.
        Annu. Rev. Genet. 1986; 20: 671-708
        • Padgett R.A.
        • Grabowski P.J.
        • Konarska M.M.
        • Seiler S.V.
        • Sharp P.A.
        Annu. Rev. Biochem. 1986; 55: 1119-1150
        • Mardon H.J.
        • Sebastio G.
        • Baralle F.E.
        Nucleic Acids Res. 1987; 15: 7725-7733
        • Cooper T.A.
        • Ordhal C.P.
        Nucleic Acids Res. 1989; 17: 7905-7921
        • Libri D.
        • Goux-Pelletan M.
        • Brody E.
        • Fiszman M.Y.
        Mol. Cell. Biol. 1990; 10: 5036-5046
        • Reed R.
        • Maniatis T.
        Cell. 1986; 46: 681-690
        • Talerico M.
        • Berget S.M.
        Mol. Cell. Biol. 1990; 10: 6299-6305
        • Zhuang Y.
        • Weiner A.
        Cell. 1986; 46: 827-835
        • Solnick D.
        • Lee S.I.
        Mol. Cell. Biol. 1987; 7: 3194-3198
        • Eperon L.P.
        • Graham I.R.
        • Griffiths A.D.
        • Eperon I.C.
        Cell. 1988; 54: 393-401
        • Libri D.
        • Marie J.
        • Brody E.
        • Fiszman M.Y.
        Nucleic Acids Res. 1989; 17: 6449-6462
        • Watakabe A.
        • Inoue K.
        • Sakamoto H.
        • Shimura Y.
        Nucleic Acids Res. 1989; 17: 8159-8169
        • Zuker M.
        • Stiegler P.
        Nucleic Acids Res. 1981; 9: 133-148
        • Freier S.M.
        • Kierzek R.
        • Jaeger J.A.
        • Sugimoto N.
        • Caruthers M.H.
        • Neilson T.
        • Turner D.H.
        Proc. Natl. Acad. Sci. U. S. A. 1986; 83: 9373-9377
        • Urlaub G.
        • Mitchell P.J.
        • Ciudad C.J.
        • Chasin L.A.
        Mol. Cell. Biol. 1989; 9: 2868-2880
        • Baserga S.J.
        • Benz E.J.
        Proc. Natl. Acad. Sci. U. S. A. 1988; 85: 2056-2060
        • Boisnard M.
        • Petrissant G.
        Biachimie. 1985; 67: 1043-11051
        • Provot C.
        • Persuy M.A.
        • Mercier J.-C.
        Biochimie. 1989; 71: 827-832
        • Grosclaude F.
        • Joudrier P.
        • Mahé M.-F.
        Ann. Genet. Sel. Anim. 1978; 10: 313-327
        • Grusby M.J.
        • Mitchell S.C.
        • Nabavi N.
        • Glimcher L.H.
        Proc. Natl. Acad. Sci. U. S. A. 1990; 87: 6897-6901
        • Stewart A.F.
        • Bonsing J.
        • Beattie C.W.
        • Shah F.
        • Willis I.M.
        • MacKinlay A.G.
        Mol. Biol. Evol. 1987; 4: 231-241
        • Boisnard M.
        • Hue D.
        • Bouniol C.
        • Mercier J.-C.
        • Gaye P.
        Eur. J. Biochem. 1991; 201: 633-641

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      Published online: March 25, 1992

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      DOI: https://doi.org/10.1016/S0021-9258(18)42674-9

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