Genetic Engineering in the Precambrian: Structure of the Chicken Triosephosphate Isomerase Gene

LITERATURE CITED

• Alber, T., and Kowasaki G.. 1982. Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae. J. Mol. Appl Genet. 1:419–434.
   PubMedGoogle Scholar
• Ambartsumyan, N. S., and Mazo A. M.. 1980. Elimination of the secondary structure effect in gel sequencing of nucleic acids. FEBS Lett. 114:265–268.
   PubMedGoogle Scholar
• Antoine, M., and Niessing J.. 1984. Intron-less globin genes in the insect Chironomus thummi thummi. Nature (London) 310:795–798.
   Google Scholar
• Artavanis-Tsakonas, S., and Harris J. I.. 1980. Primary structure of triosephosphate isomerase from B. stearothermophilus. Eur. J. Biochem. 108:599–611.
   PubMedGoogle Scholar
• Banner, D. W., Bloomer A. C., Petsko G. A., Phillips D. C., Pogson C. I., Wilson I. A., Corran P. H., Furth A. J., Milman J. D., Offord R. E., Priddle J. D., and Waley S. G.. 1975. Structure of chicken muscle triose phosphate isomerase determined crystal-lographically at 2.5 A resolution using amino acid sequence data. Nature (London) 255:609–614.
   PubMed Web of Science ®Google Scholar
• Birnboim, H. C, and Doly J.. 1979. A rapid alkaline extraction procedure for screening recombinant plasmid DNA. Nucleic Acids Res. 7:1513–1523.
   PubMed Web of Science ®Google Scholar
• Blake, C. 1978. Do genes-in-pieces imply proteins-in-pieces? Nature (London) 273:267.
   Web of Science ®Google Scholar
• Blake, C. 1983. Exons–present from the beginning? Nature (London) 306:535–537.
   PubMedGoogle Scholar
• Boyer, H. W., and Roulland-Dussoix D.. 1969. A complementation analysis of the restriction and modification, of DNA in Escherichia coli. J. Mol. Biol. 41:459–472.
   PubMed Web of Science ®Google Scholar
• Brack, C, and Tonegawa S.. 1977. Variable and constant parts of the immunoglobulin light chain gene of a mouse myeloma cell are 1250 nontranslated bases apart. Proc. Natl. Acad. Sci. USA 74:5653–5656.
   Google Scholar
• Breathnach, R., and Chambon P.. 1981. Organization and expression of eukaryotic split genes coding for proteins. Annu. Rev. Biochem. 50:349–384.
   PubMed Web of Science ®Google Scholar
• Chu, F. K., Maley G. F., Maley F., and Belfort M.. 1984. Intervening sequence in the thymidylate synthase gene of bacteriophage T4. Proc. Natl. Acad. Sci. USA 81:3049–3053.
   PubMed Web of Science ®Google Scholar
• Clewell, D. B., and Helinski D. R.. 1970. Properties of a supercoiled deoxyribonucleic acid-protein relaxation complex and strand specificity of the relaxation event. Biochemistry 9:4428–4440.
   PubMed Web of Science ®Google Scholar
• Corran, P. H., and Waley S. G.. 1975. The amino acid sequence of rabbit muscle triose phosphate isomerase. Biochem. J. 145:335–344.
   PubMedGoogle Scholar
• Craik, C. S., Sprang S., Fletterick R., and Rutter W. J.. 1982. Intron-exon splice junctions map at protein surfaces. Nature (London) 299:180–182.
   PubMed Web of Science ®Google Scholar
• Dagert, M., and Ehrlich S. D.. 1979. Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells. Gene 6:23–28.
   PubMed Web of Science ®Google Scholar
• Dayhoff, M. O., Barker W. C., and Orcutt B. C.. 1975. NBR Report No. 08710-750905. National Biomedical Research Foundation, Washington, D.C.
   Google Scholar
• deCrombrugghe, B., and Pastan I.. 1982. Structure and regulation of a collagen gene. Trends Biochem. Sci. 7:11–13.
   Google Scholar
• Doolittle, W. F. 1978. Genes in pieces: were they ever together? Nature (London) 272:581–582.
   Web of Science ®Google Scholar
• Early, P. W., Davis M. M., Kaback D. B., Davidson N., and Hood L.. 1979. Immunoglobulin heavy chain gene organization in mice: analysis of a myeloma genomic clone containing variable and alpha constant regions. Proc. Natl. Acad. Sci. USA 76:857–861.
   PubMed Web of Science ®Google Scholar
• Eifferman, F. A., Young P. R., Scott R. W., and Tilghman S. W.. 1981. Intragenic amplification and divergence in the mouse α-fetoprotein gene. Nature (London) 294:713–718.
   PubMedGoogle Scholar
• Frischauf, A., Garoff H., and Lehrach H.. 1980. A subcloning strategy for DNA sequence analysis. Nucleic Acids Res. 8:5541–5549.
   PubMedGoogle Scholar
• Furth, A. J., Milman J. D., Priddle J. D., and Offord R. E.. 1974. Studies on the subunit structure and amino acid sequence of triose phosphate isomerase from chicken breast muscle. Biochem. J. 139:11–25.
   PubMedGoogle Scholar
• Gilbert, W. 1978. Why genes in pieces? Nature (London) 271:501.
   PubMed Web of Science ®Google Scholar
• Gilbert, W. 1979. Introns and exons: playgrounds of evolution, p. 1–10. In Axel R., Maniatis T., and Fox C. F. (ed.), Eukaryotic gene regulation: ICN-UCLA Symposia on molecular and cellular biology. Academic Press, Inc., New York.
   Google Scholar
• Gö, M. 1981. Correlation of DNA exonic regions with protein structural units in hemoglobin. Nature (London) 291:90–92.
   PubMed Web of Science ®Google Scholar
• Gö, M. 1983. Modular structural units, exons, and function in chicken lysozyme. Proc. Natl. Acad. Sci. USA 80:1964–1968.
   PubMed Web of Science ®Google Scholar
• Ish-Horowicz, D., and Burke J. F.. 1981. Rapid and efficient cosmid cloning. Nucleic Acids Res. 9:2989–2998.
   PubMed Web of Science ®Google Scholar
• Kaine, B. P., Gupta R., and Woese C. R.. 1983. Putative introns in tRNA genes of prokaryotes. Proc. Natl. Acad. Sci. USA 80:3309–3312.
   PubMed Web of Science ®Google Scholar
• Kolb, E., Harris J. I., and Bridgen J.. 1974. Triose phosphate isomerase from the coelacanth. Biochem. J. 137:185–197.
   PubMedGoogle Scholar
• Lee, B., and Richards F. M.. 1971. The interpretation of protein structures: estimation of static accessibility. J. Mol. Biol. 55:379–400.
   PubMed Web of Science ®Google Scholar
• Levine, M., Muirhead H., Stammers D. K., and Stuart D. I.. 1978. Structure of pyruvate kinase and similarities with other enzymes: possible implications for protein taxonomy and evolution. Nature (London) 271:626–630.
   PubMed Web of Science ®Google Scholar
• Little, P. F. 1982. Globin pseudogenes. Cell 28:683–684.
   PubMedGoogle Scholar
• Lonberg, N., and Gilbert W.. 1985. The intron/exon structure of the chicken pyruvate kinase gene. Cell 40:81–90.
   PubMedGoogle Scholar
• Lu, J. S., Yuan P. M., and Gracy R. W.. 1984. Primary structure of human triosephosphate isomerase. J. Biol. Chem. 259: 11958–11968.
   PubMedGoogle Scholar
• Maxam, A. M., and Gilbert W.. 1980. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65:499–560.
   PubMedGoogle Scholar
• Moormann, R. J., den Dünnen J. T., Mulleners L., Andreoli P., Bloemendal H., and Schoenmakers J. G.. 1983. Strict co-linearity of genetic and protein folding domains in an intragenically duplicated rat lens gamma-crystallin gene. J. Mol. Biol. 171:353–368.
   PubMedGoogle Scholar
• Mount, S. M. 1982. A catalogue of splice junction sequences. Nucleic Acids Res. 10:461–472.
   Google Scholar
• Perler, F., Efstratiadis A., Lomedico P., Gilbert W., Kolodner R., and Dodgson J.. 1980. The evolution of genes: the chicken preproinsulin gene. Cell 20:555–566.
   PubMed Web of Science ®Google Scholar
• Pichersky, E., Gottlieb L. D., and Hess J. F.. 1984. Nucleotide sequence of the triose phosphate isomerase gene of E. coli. Mol. Gen. Genet. 195:314–320.
   PubMedGoogle Scholar
• Rigby, W. F., Diekmann M., Rhodes C., and Berg P.. 1977. Labeling DNA to high specific activity in-vitro by nick translation with DNA polymerase I. J. Mol. Biol. 113:237–251.
   PubMed Web of Science ®Google Scholar
• Sakano, H., Rogers J. H., Hueppi K., Brack C., Traunecker A., Maki R., Wall R., and Tonegawa S.. 1979. Domains and the hinge region of an immunoglobulin heavy chain are encoded in separate DNA segments. Nature (London) 277:627–633.
   PubMed Web of Science ®Google Scholar
• Shah, D. M., Hightower R. C., and Meagher R. B.. 1983. Genes encoding actin in higher plants: intron positions are highly conserved but the coding sequences are not. J. Mol. Appl. Genet. 2:111–126.
   PubMedGoogle Scholar
• Southern, E. M. 1975. Detection of specific sequences among DNA fragments separated by gel electrophoresis. J. Mol. Biol. 98:503–517.
   PubMed Web of Science ®Google Scholar
• Stammers, D. K., and Muirhead H.. 1977. Three dimensional structure for cat muscle pyruvate kinase at 3.1 A resolution. J. Mol. Biol. 112:309–316.
   PubMedGoogle Scholar
• Stein, J. P., C alter all J. F., Kristo P., Means A. R., and O'Malley B. W.. 1980. Ovomucoid intervening sequences specify functional domains and generate protein polymorphism. Cell 21:681–687.
   PubMed Web of Science ®Google Scholar
• Stone, E. M., Rothblum K., Alevy M., Kuo T., and Schwartz R. J.. 1984. The complete sequence of the chicken glyceraldehyde-3-phosphate dehydrogenase gene. Proc. Natl. Acad. Sci. USA 82:1628–1632.
   Google Scholar
• Straus, D., and Gilbert W.. 1985. Chicken triosephosphate isomerase complements and E. coli deficiency. Proc. Natl. Acad. Sci. USA 82:2014–2018.
   PubMedGoogle Scholar
• Tonegawa, S., Maxam A. M., Tizard R., Bernard O., and Gilbert W.. 1978. Sequence of a mouse germ-line gene for a variable region of an immunoglobulin light chain. Proc. Natl. Acad. Sci. USA 75:1485–1489.
   PubMed Web of Science ®Google Scholar
• Wozney, J., Hanahan D., Tate V., Boedtker H., and Doty P.. 1981. Structure of the pro alpha 2 (I) collagen gene. Nature (London) 294:129–135.
   PubMed Web of Science ®Google Scholar
• Wu, C. 1980. The 5′ ends of Drosophila heat shock genes in chromatin are hypersensitive to DNase I. Nature (London) 286:854–860.
   PubMed Web of Science ®Google Scholar
• Yamada, Y., Avvedimento V. E., Mudryj M., Ohkubo H., Vogeli G., Irani M., Pastan I., and deCrombrugghe B.. 1980. The collagen gene: evidence for its evolutionary assembly by amplification of a DNA segment containing an exon of 54 bp. Cell 22:887–892.
   PubMed Web of Science ®Google Scholar
• Zakut, R., Shani M., Givol D., Neuman S., Yaffe D., and Nudel U.. 1982. Nucleotide sequence of the rat skeletal muscle actin gene. Nature (London) 298:857–859.
   PubMedGoogle Scholar