Characterization of Two Nonallelic Pairs of Late Histone H2A and H2B Genes of the Sea Urchin: Differential Regulation in the Embryo and Tissue-Specific Expression in the Adult

LITERATURE CITED

• Angerer, L., D. DeLeon, K. Cox, R. Maxson, L. Kedes, J. Kaumeyer, E. Weinberg, and R. Angerer. 1985. Simultaneous expression of early and late histone messenger RNAs in individual cells during development of the sea urchin embryo. Dev. Biol. 112:157–166.
   PubMedGoogle Scholar
• Angerer, L. M., D. V. DeLeon, R. C. Angerer, R. M. Showman, D. E. Wells, and R. A. Raff. 1984. Delayed accumulation of maternal histone mRNA during sea urchin oogenesis. Dev. Biol. 101:477–484.
   PubMedGoogle Scholar
• Birnstiel, M. L., M. Busslinger, and K. Strub. 1985. Transcription termination and 3′ processing: the end is in site! Cell 41:349–359.
   PubMed Web of Science ®Google Scholar
• Breathnach, R., and P. Chambon. 1981. Organization and expression of eucaryotic split genes coding for proteins. Annu. Rev. Biochem. 50:349–383.
   PubMed Web of Science ®Google Scholar
• Britten, R. J., A. Cetta, and E. H. Davidson. 1978. The singlecopy DNA sequence polymorphism of the sea urchin Strongylocentrotus purpuratus. Cell 15:1175–1186.
   PubMed Web of Science ®Google Scholar
• Brush, D., J. B. Dodgson, O. Choi, P. W. Stevens, and J. D. Engel. 1985. Replacement variant histone genes contain intervening sequences. Mol. Cell. Biol. 5:1307–1317.
   PubMedGoogle Scholar
• Bryan, P. N., J. Olah, and M. L. Birnstiel. 1983. Major changes in the 5′ and 3′ chromatin structure of sea urchin histone genes accompany their activation and inactivation in development. Cell 33:843–848.
   PubMed Web of Science ®Google Scholar
• Busslinger, M., and A. Barberis. 1985. Synthesis of sperm and late histone cDNAs of the sea urchin with a primer complementary to the conserved 3′ terminal palindrome; evidence for tissue-specific and more general histone gene variants. Proc. Natl. Acad. Sci. USA 82:5676–5680.
   PubMedGoogle Scholar
• Busslinger, M., R. Portmann, and M. L. Birnstiel. 1979. A regulatory sequence near the 3′ end of sea urchin histone genes. Nucleic Acids Res. 6:2997–3008.
   PubMedGoogle Scholar
• Busslinger, M., R. Portmann, J. C. Irminger, and M. L. Birnstiel. 1980. Ubiquitous and gene-specific regulatory 5′ sequences in a sea urchin histone DNA clone coding for histone protein variants. Nucleic Acids Res. 8:957–977.
   PubMed Web of Science ®Google Scholar
• Busslinger, M., S. Rusconi, and M. L. Birnstiel. 1982. An unusual evolutionary behaviour of a sea urchin histone gene cluster. EMBO J. 1:27–33.
   PubMedGoogle Scholar
• Childs, G., C. Nocente-McGrath, T. Lieber, C. Holt, and J. A. Knowles. 1982. Sea urchin (Lytechinus pictus) late-stage H3 and H4 genes: characterisation and mapping of a clustered but nontandemly linked multigene family. Cell 31:383–393.
   PubMedGoogle Scholar
• Chirgwin, J. M., A. E. Przybyla, R. J. MacDonald, and W. J. Rutter. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294–5299.
   PubMed Web of Science ®Google Scholar
• Cleland, K. W. 1952. Heavy metals, fertilization and Cleavage in the eggs of Psammechinus miliaris. Exp. Cell Res. 4:246–248.
   Google Scholar
• Cohen, L. H., K. M. Newrock, and A. Zweidler. 1975. Stagespecific switches in histone synthesis during embryogenesis of the sea urchin. Science 190:994–997.
   PubMedGoogle Scholar
• Cox, K. H., L. M. Angerer, J. J. Lee, E. H. Davidson, and R. C. Angerer. 1986. Cell lineage-specific programs of expression of multiple actin genes during sea urchin embryogenesis. J. Mol. Biol. 188:159–172.
   PubMedGoogle Scholar
• Davidson, E. H., B. R. Hough-Evans, and R. J. Britten. 1982. Molecular biology of the sea urchin embryo. Science 217:17–26.
   PubMed Web of Science ®Google Scholar
• Falkner, F. G., and H. G. Zachau. 1984. Correct transcription of an immunoglobulin K gene requires an upstream fragment containing conserved sequence elements. Nature (London) 310:71–74.
   PubMed Web of Science ®Google Scholar
• Gick, O., A. Krämer, W. Keller, and M. L. Birnstiel. 1986. Generation of histone mRNA 3′ ends by endonucleolytic cleavageof the pre-mRNA in a snRNP-dependent in vitro reaction. EMBO J. 5:1319–1326.
   PubMedGoogle Scholar
• Graves, B. J., P. F. Johnson, and S. L. McKnight. 1986. Homologous recognition of a promoter domain common to the MSV LTR and the HSV tk gene. Cell 44:565–576.
   PubMed Web of Science ®Google Scholar
• Gross, K., E. Probst, W. Schaffner, and M. Birnstiel. 1976. Molecular analysis of the histone gene cluster of Psammechinus miliaris. I. Fractionation and identification of five individual histone mRNAs. Cell 8:455–469.
   PubMedGoogle Scholar
• Grosveld, F. G., T. Lund, E. J. Murray, A. L. Mellor, H. H. M. Dahl, and R. A. Flavell. 1982. The construction of cosmid libraries which can be used to transform eukaryotic cells. Nucleic Acids Res. 10:6715–6732.
   PubMedGoogle Scholar
• Harvey, R. P., A. J. Robins, and J. R. E. Wells. 1982. Independently evolving chicken histone H2B genes: identification of a ubiquitous H2B-specific 5′ element. Nucleic Acids Res. 10:7851–7863.
   PubMed Web of Science ®Google Scholar
• Harvey, R. P., and J. R. E. Wells. 1984. Chicken histone genes and their variants, p. 245–262. In G. Stein, J. Stein, and W. Marzluff (ed.), Histone genes and histone gene expression. John Wiley & Sons, Inc., New York.
   Google Scholar
• Hentschel, C. C., and M. L. Birnstiel. 1981. The organization and expression of histone gene families. Cell 25:301–313.
   PubMed Web of Science ®Google Scholar
• Hentschel, C., J. C. Irminger, P. Bucher, and M. L. Birnstiel. 1980. Sea urchin histone mRNA termini are located in gene regions downstream from putative regulatory sequences. Nature (London) 285:147–151.
   PubMedGoogle Scholar
• Knowles, J. A., and G. J. Childs. 1984. Temporal expression of late histone messenger RNA in the sea urchin Lytechinus pictus. Proc. Natl. Acad. Sci. USA 81:2411–2415.
   PubMedGoogle Scholar
• Mattaj, I. W., S. Lienhard, J. Jiricny, and E. M. De Robertis. 1985. An enhancer-like sequence within the Xenopus U2 gene promoter facilitates the formation of stable transcription complexes. Nature (London) 316:163–167.
   PubMed Web of Science ®Google Scholar
• Mauron, A., L. Kedes, B. R. Hough-Evans, and E. H. Davidson. 1982. Accumulation of individual histone mRNAs during embryogenesis of the sea urchin Strongylocentrotus purpuratus. Dev. Biol. 94:425–434.
   PubMedGoogle Scholar
• Maxam, A. M., and W. Gilbert. 1980. Sequencing end-labeled DNA with base-specific chemical cleavages. Methods Enzymol. 65:499–560.
   PubMedGoogle Scholar
• Maxson, R., R. Cohn, L. Kedes, and T. Mohun. 1983. Expression and organisation of histone genes. Annu. Rev. Genet. 17:239–277.
   PubMed Web of Science ®Google Scholar
• Maxson, R., T. Mohun, G. Gormezano, G. Childs, and L. Kedes. 1983 Distinct organisations and patterns of expression of early and late histone gene sets in the sea urchin. Nature (London) 301:120–125.
   PubMedGoogle Scholar
• Maxson, R.E., and F. H. Wilt. 1982. Accumulation of the early histone messenger RNAs during the development of Strongylocentrotus purpuratus. Dev. Biol. 94:435–440.
   PubMedGoogle Scholar
• Melton, D. A., P. A. Krieg, M. R. Rebagliati, T. Maniatis, K. Zinn, and M. R. Green. 1984. Efficient in vitro synthesis of biologically active RNA and RNA hybridization probes from plasmids containing a bacteriophage SP6 promoter. Nucleic Acids Res. 12:7035–7056.
   PubMed Web of Science ®Google Scholar
• Mohun, T., R. Maxson, G. Gormezano, and L. Kedes. 1985. Differential regulation of individual late histone genes during development of the sea urchin (Stronglyocentrotus purpuratus). Dev. Biol. 108:491–502.
   Google Scholar
• Nedospasov, S. A., and G. P. Georgiev. 1980. Non-random cleavage of SV40 DNA in compact minichromosomes and free in solution by M. nuclease. Biochem. Biophys. Res. Commun. 92:532–539.
   PubMed Web of Science ®Google Scholar
• Newrock, K. M., L. Cohen, M. B. Hendricks, R. J. Donnelly, and E. S. Weinberg. 1978. Stage-specific mRNAs coding for subtypes of H2A and H2B histones in the sea urchin embryo. Cell 14:327–336.
   PubMedGoogle Scholar
• Parslow, T. G., D. L. Blair, W. J. Murphy, and D. K. Granner. 1984. Structure of the 5′ ends of immunoglobulin genes: a novel conserved sequence. Proc. Natl. Acad. Sci. USA 81:2650–2654.
   PubMed Web of Science ®Google Scholar
• Pehrson, J. R., and L. H. Cohen. 1984. Embryonal histone H1 subtypes of the sea urchin Strongylocentrotus purpuratus: purification, characterisation and immunological comparison with H1 subtypes of the adult. Biochemistry 23:6761–6764.
   PubMedGoogle Scholar
• Roberts, S. B., K. E. Weisser, and G. Childs. 1984. Sequence comparison of non-allelic late histone genes and their early stage counterparts: evidence for gene conversion within the sea urchin late stage gene family. J. Mol. Biol. 174:647–662.
   PubMedGoogle Scholar
• Shott, R. J., J. J. Lee, R. J. Britten, and E. H. Davidson. 1984. Differential expression of the actin gene family of Strongylocentrotus purpuratus. Dev. Biol. 101:295–306.
   PubMedGoogle Scholar
• Smith, H. O., and M. L. Birnstiel. 1976. A simple method for DNA restriction site mapping. Nucleic Acids Res. 3:23872398.
   Google Scholar
• Sures, L., S. Levy, and L. H. Kedes. 1980. Leader sequences of Strongylocentrotus purpuratus histone mRNAs start at a unique heptanucleotide common to all five histones genes. Proc. Natl. Acad. Sci. USA 77:1265–1269.
   PubMed Web of Science ®Google Scholar
• Van Dongen, W. M. A. M., A. F. M. Moorman, and O. H. J. Destree. 1984. DNA organization and expression of Xenopus histone genes, p. 199–224. In G. Stein, J. Stein, and W. Marzluff (ed)., Histone genes and histone gene expression. John Wiley & Sons, Inc., New York.
   Google Scholar
• Weinberg, E. S., M. B. Hendricks, K. Hemminki, P. E. Kuwabara, and L. A. Farrelly. 1983. Timing and rates of synthesis of early histone mRNA in the embryo of Strongylocentrotus purpuratus. Dev. Biol. 98:117–129.
   PubMedGoogle Scholar
• Wells, D., and L. Kedes. 1985. Structure of a human cDNA: evidence that basally expressed, histone genes have intervening sequences and encode polyadenylated mRNAs. Proc. Natl. Acad. Sci. USA 82:2834–2838.
   PubMedGoogle 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
• Zweidler, A. 1984. Core histone variants of the mouse: primary structure and differential expression, p. 339–371. In G. Stein, J. Stein, and W. Marzluff (ed.), Histone genes and histone gene expression. John Wiley Sons, Inc., New York.
   Google Scholar