Skip to main content

Casein Genes and Genetic Engineering of the Caseins

  • Chapter
Genetic Engineering of Animals

Part of the book series: Basic Life Sciences ((BLSC))

Abstract

The caseins are the major proteins of milk providing needed amino acids to the suckling infant. The bovine caseins have been the most thor oughly studied and serve as the principal basis for the dairy industry. The bovine caseins are comprised of 4 major polypeptide families: αsl-, αs2-, ß-, and κ-caseins (52). They are phosphorylated to varying degrees generally containing 8, 10–13, 5, and one seryl phosphate residues per monomer, respectively. The fact that some molecules of κ-casein are also glycosylated while others do not contain carbohydrate residues gives rise to electrophoretic heterogeneity.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 39.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 54.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  1. Blackburn, D.E., A.A. Hobbs, and J.M. Rosen (1982) Rat ß-casein DNA: Sequence analysis and evolutionary comparisons. Nucl. Acids Res.10:2295–2307.

    Article  PubMed  CAS  Google Scholar 

  2. Breathnach, R., and P. Chambon (1981) Organization and expression of eukaryotic split genes coding for proteins. Ann. Rev. Biochem. 50: 349–383.

    Article  PubMed  CAS  Google Scholar 

  3. Campbell, S.M., and J.M. Rosen (1984) Comparison of the whey acidic protein genes of the rat and mouse. Nucl. Acids Res. 12:8685–8697.

    Article  PubMed  CAS  Google Scholar 

  4. Compton, J.G., W.T. Schrader, and B.W. O’Malley (1983) DNA sequence preference of the progesterone receptor. Proc. Natl. Acad. Sci., USA80:16–20.

    Article  PubMed  CAS  Google Scholar 

  5. Craig, R.K., L. Hall, D. Parker, and P. Campbell (1981) The construc-tion, identification and partial characterization of plasmids containing guinea-pig milk protein complementary DNA sequences. Biochem. J.194:989–998.

    PubMed  CAS  Google Scholar 

  6. Craig, R.K., D. Mcllreavy, and R.L. Hall (1978) Separation and partial characterization of guinea-pig caseins. Biochem. J. 173:633–641.

    PubMed  CAS  Google Scholar 

  7. Craik, C.S. (1985) Use of oligonucleotides for site-specific mutagenesis. BioTechniques 3:12–16.

    CAS  Google Scholar 

  8. Craik, C.S., W.J. Rutler, and R. Fletlerick (1983) Splice junctions: Association with variation in protein structure. Science 220:1125–1129.

    Article  PubMed  CAS  Google Scholar 

  9. Creamer, L.K., and N.F. Olson (1982) Rheological evaluation of cheddar cheese. J. Food Sci. 57:631–636.

    Article  Google Scholar 

  10. Creamer, L.K., T. Richardson, and D.A.D. Parry (1981) Secondary structure of bovine sl-and ß-casein in solution. Arch. Biochem. Biophys.211:689–696.

    Article  PubMed  CAS  Google Scholar 

  11. Dalbadie-McFarland, G.D., L.W. Cohen, A.D. Riggs, C. Morin, K. Itakura, and J.H. Richards (1982) Oligonnucleotide-directed mutagenesis as a general and powerful method for studies of protein function. Proc. Natl. Acad. Sci., USA 79:6409–6413.

    Article  PubMed  CAS  Google Scholar 

  12. Dalgleish, D.G. (1982) The enzymatic coagulation of milk. In Develop-ments in Dairy Chemistry, Vol. 1, P.F. Fox, ed. Applied Sci. Publ., New York, pp. 157–188.

    Google Scholar 

  13. Dayal, R., J. Huslmann, Y.M.L. Suard, and J.-P. Kraebenbuhl (1982) Chemical and immunochemical characterization of caseins and the major whey proteins of rabbit milk. Biochem. J. 201:71–79.

    PubMed  CAS  Google Scholar 

  14. Dayhoff, M.O. (1976) Miscellaneous proteins. In Atlas of Protein Se quence and Structure, Vol. 5 (Suppl. 2), M.O. Dayhoff, ed. National Biomedical Research Foundation, Bethesda, Maryland, pp. 261–263.

    Google Scholar 

  15. Dean, D.C., R. Gope, B.J. Knoll, M.E. Riser, and B.W. O’Malley (1984) A similar 5’-flanking region is responsible for estrogen and progesterone induction of ovalbumin gene expression. J. Biol. Chem. 259: 9967–9970.

    PubMed  CAS  Google Scholar 

  16. Eigel, W.N., J.E. Butler, C.A. Ernstrom, H.M. Farrell, Jr., V.R. Harwalkar, R. Jenness, and R. McL. Whitney (1984) Nomenclature of proteins of cow’s milk. Fifth revision. J. Dairy Sci. 67:1599.

    Article  CAS  Google Scholar 

  17. Emtage, J.S., S. Angal, M.T. Doel, T.J.R. Harris, B. Jenkins, G. Lalley, and P.A. Lome (1983) Synthesis of calf prochymosin (prorennin) in Escherichia coli. Proc. Natl. Acad. Sci., USA 80:3671–3676.

    Article  PubMed  CAS  Google Scholar 

  18. Fox, P.F. (1982) Heat-induced coagulation of milk. In Developments in Dairy Chemistry, Vol. 1, P.F. Fox, ed. Applied Sci. Publ., New York, pp. 189–228.

    Google Scholar 

  19. Gupta, P., J.M. Rosen, P. D’Eustachio, and F.M. Ruddle (1982) Localization of the casein gene family to a single mouse chromosome. J. Cell. Biol. 93:199–204.

    Article  PubMed  CAS  Google Scholar 

  20. Guyette, W.A., R.J. Matusik, and J.M. Rosen (1979) Prolactin-mediated transcriptional and posttranscriptional control of casein gene expression. Cell 17:1013–1023.

    Article  PubMed  CAS  Google Scholar 

  21. Hammer, R.E., V.G. Pursel, C.E. Rexroad, Jr., R.J. Wall, D.J. Bolt, K.M. Ebert, R.D. Palmiter, and R.L.-Brinster (1985) Production of transgenic rabbits, sheep and pigs by microinjection. Nature 315:680–683.

    Article  PubMed  CAS  Google Scholar 

  22. Hennighausen, L.G., and A.E. Sippel (1982) Characterization and cloning of the mRNAs specific for the lactating mouse mammary gland. FEBS125:131–141.

    CAS  Google Scholar 

  23. Hobbs, A.A., D.A. Richards, D.J. Kessler, and J.M. Rosen (1982) Complex hormonal regulation of rat casein gene expression. J. Biol. Chem. 257:3598–3605.

    PubMed  CAS  Google Scholar 

  24. Hobbs, A.A., and J.M. Rosen (1982) Sequence of rat and casein in mRNA: Evolutionary comparison of the calcium-dependent rat casein multigene family. Nucl. Acids Res. 10:8079–8098.

    Article  PubMed  CAS  Google Scholar 

  25. Ivanov, V.N., D.R. Kersholite, A.A. Bayer, A.A. Akhondora, G.E. Solimova, E.S. Judin-Kora, and S.I. Gorodetsky (1984) Identification of bacterial clones encoding bovine caseins by direct immunological screening of the cDNA library. Gene 32:381–388.

    Article  PubMed  CAS  Google Scholar 

  26. Jenness, R. (1982) Interspecies comparisons of milk proteins. In Developments in Dairy Chemistry, P.F. Fox, ed. Applied Sci. Publ., New York, pp. 87–114.

    Google Scholar 

  27. Jones, W.K., L.-Y. Yu-Lee, S.M. Clift, T.L. Brown, and J.M. Rosen (1985) The rat casein multigene family. III. Fine structure and evolution of the ß-casein gene. J. Biol. Chem. 260:7042–7050.

    PubMed  CAS  Google Scholar 

  28. Kinsella, J.E. (1982) Relationships between structure and functional properties of food proteins. In Food Proteins, P.F. Fox and J.J. Condon, eds. Applied Sci. Publ., New York, pp. 51–104.

    Google Scholar 

  29. Kroeker, E.M., K.F. Ng-Kwai-Hang, J.F. Hayes, and J.E. Moxeley (1985) Heritabilities of relative percentages of major bovine casein and serum proteins in test-day milk samples. J. Dairy Sci. 68:1346–1348.

    Article  CAS  Google Scholar 

  30. Kurcherlapati, R., and A.I. Skoultchi (1984) Introduction of purified genes into mammalian cells. CRC Crit. Rev. Biochem. 16:349–382.

    Article  Google Scholar 

  31. Matusik, R.J., and J.M. Rosen (1978) Prolactin induction of casein mRNA in organ culture. J. Biol. Chem. 253:2343–2347.

    PubMed  CAS  Google Scholar 

  32. Matyukov, V.S., and A.P. Urmysher (1980) Linkage of l-, ß-and k-casein loci in cattle. Genetika 16:884–886.

    CAS  Google Scholar 

  33. Maugh, II, T.H. (1984) Need a catalyst? Design an enzyme. Science223:269–271.

    Article  PubMed  Google Scholar 

  34. Maxam, A.M., and W. Gilbert (1977) A new method of sequencing DNA. Proc. Natl. Acad. Sci., USA 74:560–567.

    Article  PubMed  CAS  Google Scholar 

  35. Mehta, N.M., M.R. El-Gewely, J. Joshi, R.B. Helling, and M.R. Banerjee (1981) Cloning of various ß-casein gene sequences. Gene 15:285–288.

    Article  PubMed  CAS  Google Scholar 

  36. Mephan, T.B., P. Gage, and J.C. Mercier (1982) Biosynthesis of milk proteins. In Developments in Dairy Chemistry, Vol. 1, P.F. Fox, ed. Applied Sci. Publ., New York, pp. 115–156.

    Google Scholar 

  37. Mercier, J.-C., and P. Gaye (1982) Early events in secretion of main milk proteins: Occurrence of precursors. J. Dairy Sci. 65:299.

    Article  PubMed  CAS  Google Scholar 

  38. Mercier, J.-C., G. Haze, P. Gaye, and D. Hue (1978) Amino terminal se-quence of the precursor of ovine ß-lactoglobulin. Biochem. and Bio phys. Res. Comm. 82(4):1236–1245.

    Article  CAS  Google Scholar 

  39. Nagao, M., M. Maki, R. Sasaki, and H. Chiba (1984) Isolation and sequence analysis of bovine sl-casein cDNA clone. Agric. Biol. Chem.48(6):1663–1667.

    Article  CAS  Google Scholar 

  40. Old, R.W., and S.B. Primrose (1981) Principles of Gene Manipulation: An Introduction to Genetic Engineering, 2nd ed., University of California Press, Berkeley, California, 214 pp.

    Google Scholar 

  41. Ornitz, D.M., R.D. Palmiter, R.E. Hammer, R.L. Brinster, G.H. Swift, and R.J. MacDonald (1985) Specific expression of an elastase-human growth hormone fusion gene in pancreatic acinar cells of transgenic mice. Nature 313:600–602.

    Article  PubMed  CAS  Google Scholar 

  42. Palmiter, R.D., and R.L. Brinster (1985) Transgenic mice. Cell 41: 343–345.

    Article  PubMed  CAS  Google Scholar 

  43. Patton, S., U. Welsch, and S. Singh (1984) Genetic engineering of the mammary gland by intramammary infusion technique. J. Dairy Sci. 67: 1323–1328.

    Article  PubMed  CAS  Google Scholar 

  44. Queen, C. (1983) A vector that uses phage signals for efficient synthesis of proteins in Escherichia coli. J. Mol. Appl. Gen. 2:1–10.

    CAS  Google Scholar 

  45. Rosen, J.M., R.J. Matusik, D.A. Richards, P. Gupta, and J.R. Rodgers (1980) Multihormonal regulation of casein gene expression at the transcriptional and posttranscriptional levels in the mammary gland. Re cent Prog. Horm. Res. 36:157–193.

    CAS  Google Scholar 

  46. Rosen, J.M., S.L.C. Woo, and J.P. Comstock (1975) Regulation of casein messenger RNA during the development of the rat mammary gland. Bio chemistry 14(13):2895–2903.

    CAS  Google Scholar 

  47. Sanger, F., S. Nicklen, and A.R. Coulson (1977) DNA sequencing with chain terminating inhibitors. Proc. Natl. Acad. Sci., USA 74:5463–5468.

    Article  PubMed  CAS  Google Scholar 

  48. Sawyer, L., M.Z. Papiz, C.T. North, and E.E. Eliopoulos (1985) Structure and function of bovine ß-lactoglobulin. Biochem. Soc. Transac.13:265–266.

    CAS  Google Scholar 

  49. Schmidt, D.G. (1982) Association of caseins and casein micelle structure. In Developments in Dairy Chemistry, Vol. 1, P.F. Fox, ed. Applied Sci. Publ., New York, pp. 61–86.

    Google Scholar 

  50. Stewart, A.F., I.M. Willis, and A.G. MacKinlay (1984) Nucleotide sequences of bovine sl-and -casein cDNAs. Nucl. Acids Res. 12(9): 3895–3907.

    Article  PubMed  CAS  Google Scholar 

  51. Suard, Y.M.L., M. Tosi, and J.P. Kraehenbuhl (1982) Characterization of the translation products of the major mRNA species from rabbit lactating mammary glands and construction of bacterial recombinants containing casein and lactalbumin complementary DNA. Biochem. J.201:81–90.

    PubMed  CAS  Google Scholar 

  52. Swaisgood, H.E. (1982) Chemistry of milk protein. In Developments in Dairy Chemistry, Vol. 1, P.F. Fox, ed. Applied Sci. Publ., New York, pp. 1–60.

    Google Scholar 

  53. Swift, G.H., R.E. Hammer, R.J. MacDonald, and R.L. Brinster (1984) Tissue-specific expression of the rat pancreatic elastase I gene in transgenic mice. Cell 38:639–646.

    Article  PubMed  CAS  Google Scholar 

  54. Topper, Y.S. (1970) Multiple hormone interactions in the development of mammary gland in vitro. Recent Prog. Horm. Res. 26:287–308.

    PubMed  CAS  Google Scholar 

  55. Ulmer, K. (1983) Protein engineering. Science 219:666–669.

    Article  PubMed  CAS  Google Scholar 

  56. Walstra, P., and R. Jenness (1984) Dairy Chemistry and Physics, John Wiley and Sons, New York, pp. 359–361.

    Google Scholar 

  57. Watson, J.D., J. Tooze, and D.T. Kurtz (1983) Recombinant DNA: A Short Course, W.H. Freeman and Co., New York, 260 pp.

    Google Scholar 

  58. Wilkinson, A.J., A.F. Fersht, D.M. Blow, P. Carter, and G. Winter (1984) A large increase in enzyme-substrate affinity by protein engi-neering. Nature 307:187–188.

    Article  PubMed  CAS  Google Scholar 

  59. Willis, I.M., A.F. Stewart, A. Caputo, A.R. Thompson, and A.G. Mackinlay (1982) Construction and identification by partial nucleotide sequence analysis of bovine casein and ß-lactoglobulin cDNA clones. DNA l(4):375–386.

    Article  Google Scholar 

  60. Yu-Lee, L.-Y., and J.M. Rosen (1983) The rat casein multigene family. I. Fine structure of the casein gene. J. Biol Chem. 258:10794–10804.

    PubMed  CAS  Google Scholar 

  61. Zoller, M.J., and M. Smith (1983) Oligonucleotide-directed mutagenesis of DNA fragments cloned into M13 vectors. Methods in Enzymology 100: 468–478.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Editor information

Editors and Affiliations

Rights and permissions

Reprints and permissions

Copyright information

© 1986 Plenum Press, New York

About this chapter

Cite this chapter

Kang, Y., Jimenez-Flores, R., Richardson, T. (1986). Casein Genes and Genetic Engineering of the Caseins. In: Evans, J.W., Hollaender, A., Wilson, C.M. (eds) Genetic Engineering of Animals. Basic Life Sciences. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5110-8_9

Download citation

  • DOI: https://doi.org/10.1007/978-1-4684-5110-8_9

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4684-5112-2

  • Online ISBN: 978-1-4684-5110-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics