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. 1980 Oct;77(10):5879–5883. doi: 10.1073/pnas.77.10.5879

Comparison of two delta-crystallin genes in the chicken.

R E Jones, S P Bhat, M A Sullivan, J Piatigorsky
PMCID: PMC350175  PMID: 6255468

Abstract

Restriction endonuclease mapping and electron microscopy established that there are at least two nonallelic delta-crystallin genes in the chicken. The structure of a complete delta-crystallin gene has been deduced by analysis of five cloned fragments from the chicken genome. Fifteen intervening sequences compose approximately 80% of this gene; the other gene contains at least 14 intervening sequences. The mRNA gene sequences appear to be similar; at least 60% divergence was found between the intervening sequences of the two delta-crystallin genes. Insertions or deletions or both appear to be major events responsible for these differences.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bhat S. P., Jones R. E., Sullivan M. A., Piatigorsky J. Chicken lens crystallin DNA sequences show at least two delta-crystallin genes. Nature. 1980 Mar 20;284(5753):234–238. doi: 10.1038/284234a0. [DOI] [PubMed] [Google Scholar]
  2. Bhat S. P., Piatigorsky J. Molecular cloning and partial characterization of delta-crystallin cDNA sequences in a bacterial plasmid. Proc Natl Acad Sci U S A. 1979 Jul;76(7):3299–3303. doi: 10.1073/pnas.76.7.3299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Genis-Galves J. M., Maisel H., Castro J. Changes in chick lens proteins with aging. Exp Eye Res. 1968 Oct;7(4):593–602. doi: 10.1016/s0014-4835(68)80014-4. [DOI] [PubMed] [Google Scholar]
  4. Konkel D. A., Maizel J. V., Jr, Leder P. The evolution and sequence comparison of two recently diverged mouse chromosomal beta--globin genes. Cell. 1979 Nov;18(3):865–873. doi: 10.1016/0092-8674(79)90138-7. [DOI] [PubMed] [Google Scholar]
  5. Lomedico P., Rosenthal N., Efstratidadis A., Gilbert W., Kolodner R., Tizard R. The structure and evolution of the two nonallelic rat preproinsulin genes. Cell. 1979 Oct;18(2):545–558. doi: 10.1016/0092-8674(79)90071-0. [DOI] [PubMed] [Google Scholar]
  6. Maniatis T., Hardison R. C., Lacy E., Lauer J., O'Connell C., Quon D., Sim G. K., Efstratiadis A. The isolation of structural genes from libraries of eucaryotic DNA. Cell. 1978 Oct;15(2):687–701. doi: 10.1016/0092-8674(78)90036-3. [DOI] [PubMed] [Google Scholar]
  7. Maniatis T., Jeffrey A., Kleid D. G. Nucleotide sequence of the rightward operator of phage lambda. Proc Natl Acad Sci U S A. 1975 Mar;72(3):1184–1188. doi: 10.1073/pnas.72.3.1184. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. McDonell M. W., Simon M. N., Studier F. W. Analysis of restriction fragments of T7 DNA and determination of molecular weights by electrophoresis in neutral and alkaline gels. J Mol Biol. 1977 Feb 15;110(1):119–146. doi: 10.1016/s0022-2836(77)80102-2. [DOI] [PubMed] [Google Scholar]
  9. Nishioka Y., Leder P. The complete sequence of a chromosomal mouse alpha--globin gene reveals elements conserved throughout vertebrate evolution. Cell. 1979 Nov;18(3):875–882. doi: 10.1016/0092-8674(79)90139-9. [DOI] [PubMed] [Google Scholar]
  10. Piatigorsky J. Subunit composition of delta-crystallin from embryonic chick lens. Analysis of methionine-containing tryptic peptides and cyanogen bromide peptides. J Biol Chem. 1976 Jul 25;251(14):4416–4420. [PubMed] [Google Scholar]
  11. Piatigorsky J., Webster H. D., Craig S. P. Protein synthesis and ultrastructure during the formation of embryonic chick lens fibers in vivo and in vitro. Dev Biol. 1972 Feb;27(2):176–189. doi: 10.1016/0012-1606(72)90096-6. [DOI] [PubMed] [Google Scholar]
  12. Piatigorsky J., Zelenka P., Simpson R. T. Molecular weight and subunit structure of delta-crystallin from embryonic chick lens fibers. Exp Eye Res. 1974 May;18(5):435–446. doi: 10.1016/0014-4835(74)90080-3. [DOI] [PubMed] [Google Scholar]
  13. RABAEY M. Electrophoretic and immunoelectrophoretic studies on the soluble proteins in the developing lens of birds. Exp Eye Res. 1962 Jun;1:310–316. doi: 10.1016/s0014-4835(62)80017-7. [DOI] [PubMed] [Google Scholar]
  14. Reszelbach R., Shinohara T., Piatigorsky J. Resolution of two distinct embryonic chick delta-crystallin bands by polyacrylamide gel electrophoresis in the presence of sodium dodecyl sulfate and urea. Exp Eye Res. 1977 Dec;25(6):583–593. doi: 10.1016/0014-4835(77)90137-3. [DOI] [PubMed] [Google Scholar]
  15. Shinohara T., Piatigorsky J. Anion and cation effects on delta-crystallin synthesis in the cultured embryonic chick lens and in a reticulocyte lysate. Exp Eye Res. 1980 Apr;30(4):351–360. doi: 10.1016/0014-4835(80)90050-0. [DOI] [PubMed] [Google Scholar]
  16. Shinohara T., Piatigorsky J. Quantitation of delta-crystallin messenger RNA during lens induction in chick embryos. Proc Natl Acad Sci U S A. 1976 Aug;73(8):2808–2812. doi: 10.1073/pnas.73.8.2808. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Shinohara T., Piatigorsky J. Regulation of protein synthesis, intracellular electrolytes and cataract formation in vitro. Nature. 1977 Dec 1;270(5636):406–411. doi: 10.1038/270406a0. [DOI] [PubMed] [Google Scholar]
  18. Shinohara T., Reszelbach R., Piatigorsky J. Two tryptic peptide differences among the subunits of delta-crystallin of the embryonic chick lens. Exp Eye Res. 1980 Apr;30(4):361–370. doi: 10.1016/0014-4835(80)90051-2. [DOI] [PubMed] [Google Scholar]
  19. Southern E. M. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J Mol Biol. 1975 Nov 5;98(3):503–517. doi: 10.1016/s0022-2836(75)80083-0. [DOI] [PubMed] [Google Scholar]
  20. Tiemeier D. C., Tilghman S. M., Leder P. Purification and cloning of a mouse ribosomal gene fragment in coliphage lambda. Gene. 1977;2(3-4):173–191. doi: 10.1016/0378-1119(77)90016-6. [DOI] [PubMed] [Google Scholar]
  21. Williams L. A., Piatigorsky J. Comparative and evolutionary aspects of delta-crystallin in the vertebrate lens. Eur J Biochem. 1979 Oct 15;100(2):349–357. doi: 10.1111/j.1432-1033.1979.tb04177.x. [DOI] [PubMed] [Google Scholar]
  22. Yoshida K., Katoh A. Crystallin synthesis by chick lens. II. Changes in synthetic activities of epithelial and fiber cells during embryonic development. Exp Eye Res. 1971 Mar;11(2):184–194. doi: 10.1016/s0014-4835(71)80022-2. [DOI] [PubMed] [Google Scholar]
  23. Young N. S., Benz E. J., Jr, Kantor J. A., Kretschmer P., Nienhuis A. W. Hemoglobin switching in sheep: only the gamma gene is in the active conformation in fetal liver but all the beta and gamma genes are in the active conformation in bone marrow. Proc Natl Acad Sci U S A. 1978 Dec;75(12):5884–5888. doi: 10.1073/pnas.75.12.5884. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Zwaan J., Ikeda A. Macromolecular events during differentiation of the chicken lens. Exp Eye Res. 1968 Apr;7(2):301–311. doi: 10.1016/s0014-4835(68)80081-8. [DOI] [PubMed] [Google Scholar]

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