Two types of polyadenated mRNAs are synthesized from Drosophila replication-dependent histone genes

European Journal of Biochemistry

Volumn 244, Issue 2, 1997, Pages 294-300

  Akhmanova, Anna ^a   Miedema, Koos ^a   Kremer, Hannie ^a   Hennig, Wolfgang ^a,b  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^b JOHANNES GUTENBERG UNIVERSITY   (Germany)

Author keywords

Drosophila; Histone; Polyadenylation; Spermatogenesis; Testis

Indexed keywords

HISTONE; HISTONE H2B; HISTONE H3; HISTONE H4; MESSENGER RNA;

ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DROSOPHILA MELANOGASTER; GENETIC ANALYSIS; HISTOCHEMISTRY; NONHUMAN; NORTHERN BLOTTING; POLYADENYLATION; PRIORITY JOURNAL; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; RNA ANALYSIS; TESTIS;

ANIMALIA; DROSOPHILA MELANOGASTER; MELANOGASTER;

EID: 0031051014     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.00294.x     Document Type: Article

References (45)

1. Akhmanova, A. S., Bindels, P. C. T., Xu, J., Miedema, K., Kremer, H. & Hennig, W. (1995) Structure and expression of histone H3.3 genes in Drosophila melanogaster and Drosophila hydei, Genome 38, 586-600.
2. Akhmanova, A., Miedema, K. & Hennig, W. (1996) Identification and characterization of the Drosophila histone H4 replacement gene, FEBS Lett. 388, 219-222.
3. Anderson, K. V. & Lengyel, J. A. (1984) Histone gene expression in Drosophila development: multiple levels of gene regulation, in Histone genes. Structure, organization and regulation (Stein, G. S., Stein, J. L. & Marzluff, W. F., eds) pp. 135-161, John Wiley & Sons, New York.
4. Ballantine, J. E. & Woodland, H. R. (1985) Polyadenylation of histone mRNA in Xenopus oocytes and embryos, FEBS Lett. 180, 224-228.
5. Birnstiel, M. L., Busslinger, M. & Strub, K. (1985) Transcription termination and 3′ processing: the end is in site, Cell 41, 349-359.
6. Brawerman, G. (1981) The role of the poly(A) sequence in mammalian RNA, CRC Crit. Rev. Biochem. 10, 1-38.
7. Challoner, P. B., Moss, S. B. & Groudine, M. (1989) Expression of replication-dependent histone genes in avian spermatids involves an alternate pathway of mRNA 3′-end formation, Mol. Cell. Biol. 9, 902-913.
8. Cheng, G. H., Nandi, A., Clerk, S. & Skoultchi, A. I. (1989) Different 3′-end processing produces two independently regulated mRNAs from a single H1 histone gene, Proc. Natl Acad. Sci. USA 86, 7002-7006.
9. Chirgwin, J. M., Przybyla, A. E., MacDonald, R. J. & Rutter, W. J. (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease, Biochemistry 18, 5294-5299.
10. Eckner, R., Ellmeier, W. & Birnstiel, M. L. (1991) Mature mRNA 3′ end formation stimulates RNA export from the nucleus, EMBO J. 10, 3513-3522.
11. Frohman, M. A. (1990) RACE: rapid amplification of cDNA ends, in PCR protocols: a guide to methods and applications (Innis, M. A., Gelfand, D. H., Sninsky, J. J. & White, T. J., eds) pp. 28-38, Academic Press, San Diego.
12. Graves, R. A., Pandey, N. B., Chodchoy, N. & Marzluff, W. F. (1987) Translation is required for regulation of histone mRNA degradation, Cell. 48, 615-626.
13. Hennig, W. (1967) Untersuchungen zur Struktur und Funktion des Lampenbürsten-Y-Chromosoms in der Spermatogenese von Drosophila, Chromosoma 22, 294-357.
14. Jackson, R. J. & Standart, N. (1990) Do the poly(A) tail and 3′ untranslated region control mRNA translation? Cell 82, 15-24.
15. Keller, W. (1995) No end yet to messenger RNA 3′ processing, Cell 81, 829-832.
16. Kirsh, A. L., Groudine, M. & Challoner, P. B. (1989) Polyadenylation and U7 snRNP-mediated cleavage: alternative modes of RNA 3′ processing in two avian histone H1 genes, Genes & Dev. 3, 2172-2179.
17. Kremer, H. & Hennig, W. (1990) Isolation and characterization of a Drosophila hydei histone DNA repeat unit, Nucleic Acids Res. 18, 1573-1580.
18. Levine, B. J., Chodchoy, N., Marzluff, W. F. & Skoultchi, A. I. (1987) Coupling of replication type histone mRNA levels to DNA synthesis requires the stem-loop sequence at the 3′ end of the mRNA, Proc. Natl Acad. Sci. USA 84, 6189-6193.
19. Liu, X. & Gorovsky, M. A. (1993) Mapping the 5′ and 3′ ends of Tetrahymena thermophila mRNAs using RNA ligase mediated amplification of cDNA ends (RLM-RACE), Nucleic Acids Res. 21, 4954-4960.
20. Mannironi, C., Bonner, W. M. & Hatch, C. L. (1989) H2A.X, a histone isoprotein with a conserved C-terminal sequence, is encoded by a novel mRNA with both DNA replication type and polyA 3′ processing signals, Nucleic Acids Res. 17, 9113-9126.
21. Marzluff, W. F. & Pandey, N. B. (1988) Multiple regulatory steps control histone mRNA concentrations, Trends Biochem. Sci. 13, 49-52.
22. Marzluff, W. F. (1992) Histone 3′ ends: essential and regulatory functions, Gene Expr. 2, 93-97.
23. Matsuo, Y. & Yamazaki, T. (1989) tRNA derived insertion element in histone gene repeating unit of Drosophila melanogaster, Nucleic Acids Res. 17, 225-238.
24. Moss, S. B., Ferry, R. A. & Groudine, M. (1994) An alternative pathway of histone mRNA 3′ end formation in mouse round spermatids, Nucleic Acids Res. 22, 3160-3166.
25. Mowry, K. L., Oh, R. & Steitz, J. A. (1989) Each of the conserved sequence elements flanking the cleavage site of mammalian histone pre-mRNAs has a distinct role in the 3′-end processing reaction, Mol. Cell. Biol. 9, 3105-3108.
26. Munroe, D. & Jacobson, A. (1990) Tales of poly(A): a review, Gene (Amst.) 91, 151-158.
27. Nagata, T., Kato, T., Morita, T., Nozaki, M., Kubota, H., Yagi, H. & Matsushiro, A. (1991) Polyadenylated and 3′ processed mRNAs are transcribed from the mouse histone H2A.X gene, Nucleic Acids Res. 19, 2441-2447.
28. Nesic, D. & Maquat, L. E. (1994) Upstream introns influence the efficiency of final intron removal and RNA 3′-end formation, Gene Dev. 8, 363-375.
29. Osley, M. A. (1991) The regulation of histone synthesis in the cell cycle, Annu. Rev. Biochem. 60, 827-861.
30. Pandey, N. B. & Marzluff, W. F. (1987) The stem-loop structure at the 3′ end of histone mRNA is necessary and sufficient for regulation of histone mRNA stability, Mol. Cell. Biol. 7, 4557-4559.
31. Pandey, N. B., Chodchoy, N., Liu, T.-J. & Marzluff, W. F. (1990) Introns in histone genes alter the distribution of 3′ ends, Nucleic Acids Res. 18, 3161-3170.
32. Ross, J., Peltz, S. W., Kobs, G. & Brewer, G. (1986) Histone mRNA degradation in vivo: the first detectable step occurs at or near the 3′ terminus, Mol. Cell. Biol. 6, 4362-4371.
33. Ruderman, J. V., Woodland, H. R. & Sturgess, E. A. (1979) Modulations of histone messenger RNA during the early development of Xenopus laevis, Dev. Biol. 71, 71-82.
34. Sachs, A. B. (1993) Messenger RNA degradation in eukaryotes, Cell 74, 413-421.
35. Schümperli, D. (1986) Cell-cycle regulation of histone gene expression, Cell 45, 471-472.
36. Schümperli, D. (1988) Multilevel regulation of replication-dependent histone genes, Trends Genet. 4, 187-191.
37. Sheets, M. D., Ogg, S. C. & Wickens, M. P. (1990) Point mutations in AAUAAA and the poly(A) addition site: effects on the accuracy and efficiency of cleavage and polyadenylation in vitro, Nucleic Acids Res. 18, 5799-5805.
38. Sun, J., Pilch, D. R. & Marzluff, W. F. (1992) The histone mRNA 3′ end is required for localization of histone mRNA to polyribosomes, Nucleic Acids Res. 20, 6057-6066.
39. Throckmorton, L. H. (1975) The phylogeny, ecology and geography of Drosophila, in Handbook of genetics: Invertebrates of genetic interest (King, R. C., ed.) vol. 3, pp. 421-469, Plenum Press, New York.
40. Vasserot, A. P., Schaufele, F. J. & Birnstiel, M. L. (1989) Conserved terminal hairpin sequences of histone mRNA precursors are not involved in duplex formation with the U7 RNA but act as a target site for a distinct processing factor, Proc. Natl Acad. Sci. USA 86, 4345-4349.
41. Wahle, E. & Keller, W. (1992) The biochemistry of 3′-end cleavage and polyadenylation of messenger RNA precursors, Annu. Rev. Biochem. 61, 419-440.
42. Wahle, E. (1995) 3′-End cleavage and polyadenylation of mRNA precursors, Biochim. Biophys. Acta 1261, 183-194.
43. Williams, A. S., Ingledue, T. C., Kay, B. K. & Marzluff, W. F. (1994) Changes in the stem-loop at the 3′ terminus of histone mRNA affect its nucleocytoplasmic transport and cytoplasmic regulation, Nucleic Acids Res. 22, 4660-4666.
44. Williams, A. S. & Marzluff, W. F. (1995) The sequence of the stem and flanking sequences at the 3′ end of histone mRNA are critical determinants for the binding of the stem-loop binding protein, Nucleic Acids Res. 23, 654-662.
45. Zweidler, A. (1984) Core histone variants of the mouse: primary structure and differential expression in histone genes, in Histone genes. Structure, organization and regulation (Stein, G. S., Stein, J. L. & Marzluff, W. F., eds) pp. 339-371, John Wiley & Sons, New York.