Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1986 May;83(9):2855–2859. doi: 10.1073/pnas.83.9.2855

Intron insertions and deletions in the beta/gamma-crystallin gene family: the rat beta B1 gene.

J T den Dunnen, R J Moormann, N H Lubsen, J G Schoenmakers
PMCID: PMC323405  PMID: 3458246

Abstract

The rat beta B1-crystallin gene is 13.6 kilobases long and contains six exons. The coding region of the gene is divided over five exons. Each functional entity of the protein is encoded by a separate exon except for the carboxyl-terminal extension, which shares the last exon with the fourth protein motif. Exon 2, encoding the amino-terminal extension of the protein, contains two direct repeats with an overall homology of 68% to the rat brain identifier sequence. A copy of the brain identifier sequence is also found in the 3'-flanking region of the gene. The start site of the mRNA was located by S1 nuclease mapping and analysis of the RNA sequence. The 5' end of the gene was shown to be a 27-base-pair noncoding exon, which is separated from the translation start site by 1.36 kilobases of intronic DNA. The 5'-flanking sequence of the beta B1 gene is highly homologous to that of a gamma-crystallin gene.

Full text

PDF
2855

Images in this article

2856Image
on p.2856
2856Image
on p.2856

Selected References

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

  1. Blake C. Exons--present from the beginning? Nature. 1983 Dec 8;306(5943):535–537. doi: 10.1038/306535a0. [DOI] [PubMed] [Google Scholar]
  2. Bloemendal H. Lens proteins. CRC Crit Rev Biochem. 1982;12(1):1–38. doi: 10.3109/10409238209105849. [DOI] [PubMed] [Google Scholar]
  3. Blundell T., Lindley P., Miller L., Moss D., Slingsby C., Tickle I., Turnell B., Wistow G. The molecular structure and stability of the eye lens: x-ray analysis of gamma-crystallin II. Nature. 1981 Feb 26;289(5800):771–777. doi: 10.1038/289771a0. [DOI] [PubMed] [Google Scholar]
  4. Bower D. J., Errington L. H., Cooper D. N., Morris S., Clayton R. M. Chicken lens delta-crystallin gene expression and methylation in several non-lens tissues. Nucleic Acids Res. 1983 May 11;11(9):2513–2527. doi: 10.1093/nar/11.9.2513. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Driessen H. P., Herbrink P., Bloemendal H., de Jong W. W. Primary structure of the bovine beta-crystallin Bp chain. Internal duplication and homology with gamma-crystallin. Eur J Biochem. 1981 Dec;121(1):83–91. doi: 10.1111/j.1432-1033.1981.tb06433.x. [DOI] [PubMed] [Google Scholar]
  6. Inana G., Piatigorsky J., Norman B., Slingsby C., Blundell T. Gene and protein structure of a beta-crystallin polypeptide in murine lens: relationship of exons and structural motifs. Nature. 1983 Mar 24;302(5906):310–315. doi: 10.1038/302310a0. [DOI] [PubMed] [Google Scholar]
  7. King C. R., Piatigorsky J. Alternative RNA splicing of the murine alpha A-crystallin gene: protein-coding information within an intron. Cell. 1983 Mar;32(3):707–712. doi: 10.1016/0092-8674(83)90056-9. [DOI] [PubMed] [Google Scholar]
  8. Krayev A. S., Markusheva T. V., Kramerov D. A., Ryskov A. P., Skryabin K. G., Bayev A. A., Georgiev G. P. Ubiquitous transposon-like repeats B1 and B2 of the mouse genome: B2 sequencing. Nucleic Acids Res. 1982 Dec 11;10(23):7461–7475. doi: 10.1093/nar/10.23.7461. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lok S., Tsui L. C., Shinohara T., Piatigorsky J., Gold R., Breitman M. Analysis of the mouse gamma-crystallin gene family: assignment of multiple cDNAs to discrete genomic sequences and characterization of a representative gene. Nucleic Acids Res. 1984 Jun 11;12(11):4517–4529. doi: 10.1093/nar/12.11.4517. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Milner R. J., Bloom F. E., Lai C., Lerner R. A., Sutcliffe J. G. Brain-specific genes have identifier sequences in their introns. Proc Natl Acad Sci U S A. 1984 Feb;81(3):713–717. doi: 10.1073/pnas.81.3.713. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Moormann R. J., Jongbloed R., Schoenmakers J. G. Isolation and characterization of beta- and gamma-crystallin genes from rat genomic cosmid libraries. Gene. 1984 Jul-Aug;29(1-2):1–9. doi: 10.1016/0378-1119(84)90159-8. [DOI] [PubMed] [Google Scholar]
  12. Moormann R. J., den Dunnen J. T., Heuyerjans J., Jongbloed R. J., van Leen R. W., Lubsen N. H., Schoenmakers J. G. Characterization of the rat gamma-crystallin gene family and its expression in the eye lens. J Mol Biol. 1985 Apr 5;182(3):419–430. doi: 10.1016/0022-2836(85)90201-3. [DOI] [PubMed] [Google Scholar]
  13. Moormann R. J., den Dunnen J. T., Mulleners L., Andreoli P., Bloemendal H., Schoenmakers J. G. Strict co-linearity of genetic and protein folding domains in an intragenically duplicated rat lens gamma-crystallin gene. J Mol Biol. 1983 Dec 25;171(4):353–368. doi: 10.1016/0022-2836(83)90034-7. [DOI] [PubMed] [Google Scholar]
  14. Moos M., Gallwitz D. Structure of two human beta-actin-related processed genes one of which is located next to a simple repetitive sequence. EMBO J. 1983;2(5):757–761. doi: 10.1002/j.1460-2075.1983.tb01496.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Owens G. P., Chaudhari N., Hahn W. E. Brain "identifier sequence" is not restricted to brain: similar abundance in nuclear RNA of other organs. Science. 1985 Sep 20;229(4719):1263–1265. doi: 10.1126/science.2412293. [DOI] [PubMed] [Google Scholar]
  16. Piatigorsky J. Lens differentiation in vertebrates. A review of cellular and molecular features. Differentiation. 1981;19(3):134–153. doi: 10.1111/j.1432-0436.1981.tb01141.x. [DOI] [PubMed] [Google Scholar]
  17. Tanaka T., Ohkubo H., Nakanishi S. Common structural organization of the angiotensinogen and the alpha 1-antitrypsin genes. J Biol Chem. 1984 Jul 10;259(13):8063–8065. [PubMed] [Google Scholar]
  18. Walker P., Brown-Luedi M., Germond J. E., Wahli W., Meijlink F. C., van het Schip A. D., Roelink H., Gruber M., Ab G. Sequence homologies within the 5' end region of the estrogen-controlled vitellogenin gene in Xenopus and chicken. EMBO J. 1983;2(12):2271–2279. doi: 10.1002/j.1460-2075.1983.tb01734.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. den Dunnen J. T., Moormann R. J., Cremers F. P., Schoenmakers J. G. Two human gamma-crystallin genes are linked and riddled with Alu-repeats. Gene. 1985;38(1-3):197–204. doi: 10.1016/0378-1119(85)90218-5. [DOI] [PubMed] [Google Scholar]
  20. den Dunnen J. T., Moormann R. J., Schoenmakers J. G. Rat lens beta-crystallins are internally duplicated and homologous to gamma-crystallins. Biochim Biophys Acta. 1985 Apr 19;824(4):295–303. doi: 10.1016/0167-4781(85)90035-1. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES