The protein that binds the 3' end of histone mRNA: A novel RNA-binding protein required for histone pre-mRNA processing

Genes and Development

Volumn 10, Issue 23, 1996, Pages 3028-3040

  Wang, Zeng Feng ^a   Whitfield, Michael L ^a   Ingledue III, Thomas C ^a   Dominski, Zbigniew ^a   Marzluff, William F ^a  

^a UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

3' end; Histone mRNA; pre mRNA processing; stem loop binding protein

Indexed keywords

COMPLEMENTARY DNA; HISTONE; MESSENGER RNA; MESSENGER RNA PRECURSOR; RNA BINDING PROTEIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DNA SEQUENCE; FROG; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; RNA BINDING; RNA PROCESSING;

ANIMALIA; ANURA;

EID: 0029839610     PISSN: 08909369     EISSN: None     Source Type: Journal    
DOI: 10.1101/gad.10.23.3028     Document Type: Article

References (39)

1. Bernstein, P. and J. Ross. 1989. Poly(A), poly(A) binding protein and the regulation of mRNA stability. Trends Biochem. Sci. 14: 373-377.
2. Bond, U.M., T.A. Yario, and J.A. Steitz. 1991. Multiple processing-defective mutations in a mammalian histone premessenger RNA are suppressed by compensatory changes in U7 RNA both in vivo and in vitro. Genes & Dev. 5: 1709-1722.
3. Burd, C.G. and G. Dreyfuss. 1994. Conserved structures and diversity of functions of RNA-binding proteins. Science 265: 615-621.
4. Burd, C.G., E.L. Matunis, and G. Dreyfuss. 1991. The multiple RNA-binding domains of the mRNA poly(A)-binding protein have different RNA-binding activities. Mol. Cell. Biol. 11: 3419-3424.
5. Cotten, M., O. Gick, A. Vasserot, G. Schaffner, and M.L. Birnstiel. 1988. Specific contacts between mammalian U7 snRNA and histone precursor RNA are indispensable for the in vitro RNA processing reaction. EMBO J. 7: 801-808.
6. Decker, C.J. and R. Parker. 1994. Mechanisms of mRNA degradation in eukaryotes. Trends Biochem. Sci. 19: 336-340.
7. Dominski, Z., J. Sumerel, R.J. Hanson, and W.F. Marzluff. 1995. The polyribosomal protein bound to the 3′ end of histone mRNA can function in histone pre-mRNA processing. RNA 1: 915-923.
8. Draper, D.E. 1995. Protein-RNA recognition. Annu. Rev. Biochem. 64: 593-620.
9. Gick, O., A. Krämer, A. Vasserot, and M.L. Birnstiel. 1987. Heat-labile regulatory factor is required for 3′ processing of histone precursor mRNAs. Proc. Natl. Acad. Sci. 84: 8937-8940.
10. Hanson, R.J., J.-H. Sun, D.G. Willis, and W.F. Marzluff. 1996. Efficient extraction and partial purification of the polyribosomal-associated stem-loop binding protein bound to the 3′ end of histone mRNA. Biochemistry 35: 2146-2156.
11. Harlow E. and D. Lane. 1988. Storing and purifying antibodies. In Antibodies: A laboratory manual, pp. 283-318. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
12. Harris, M.E., R. Böhni, M.H. Schneiderman, L. Ramamurthy, D. Schümperli, and W.F. Marzluff. 1991. Regulation of histone mRNA in the unperturbed cell cycle: Evidence suggesting control at two posttranscriptional steps. Mol. Cell. Biol. 11: 2416-2424.
13. Heintz, N. 1991. The regulation of histone gene expression during the cell cycle. Biochim. Biophys. Acta Gene Struct. Expression 1088: 327-339.
14. Jackson, R.J. and N. Standart. 1990. Do the poly(A) tail and 3′ untranslated region control mRNA translation? Cell 62: 15-24.
15. Kalland, K.-H., A.M. Szilvay, K.A. Brokstad, W. Saetrevik, and G. Haukenes. 1994. The human immunodeficiency virus type 1 Rev protein shuttles between the cytoplasm and nuclear compartments. Mol. Cell. Biol. 14: 7436-7444.
16. McCombie, W.R., A. Martin-Gallardo, J.D. Gocayne, M. FitzGerald, M. Dubnick, J.M. Kelley, L. Castilla, L.I. Liu, S. Wallace, S. Trapp, et al. 1992. Expressed genes, Alu repeats and polymorphisms in cosmids sequenced from chromosome 4p16.3. Nature Genet. 1: 348-353.
17. Martin, F., A. Schaller, S. Egilte, D. Schümperli, and B. Muller. 1997. The gene for histone RNA hairpin-binding protein is located on human chromosome 4 and encodes a novel type of RNA-binding protein. EMBO J. (in press).
18. Marzluff, W.F. and N.B. Pandey. 1988. Multiple levels of regulation of histone mRNA concentrations. Trends Biochem. Sci. 13: 49-52.
19. Melin, L., D. Soldati, R. Mital, A. Streit, and D. Schümperli. 1992. Biochemical demonstration of complex formation of histone pre-mRNA with U7 small nuclear ribonucleoprotein and hairpin binding factors. EMBO J. 11: 691-697.
20. Michael, W.M., M.Y. Choi, and G. Dreyfuss. 1995. A nuclear export signal in hnRNP A1 : A signal-mediated, temperature-dependent nuclear protein export pathway. Cell 83: 415-422.
21. Mowry, K.L. and J.A. Steitz. 1987a. Both conserved signals on mammalian histone pre-mRNAs associate with small nuclear ribonucleoproteins during 3′ end formation in vitro. Mol. Cell. Biol. 7: 1663-1672.
22. _. 1987b. Identification of the human U7 snRNP as one of several factors involved in the 3′ end maturation of histone premessenger RNA's. Science 238: 1682-1687.
23. Mowry, K.L., R. Oh, and J.A. Steitz. 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.
24. Nietfeld, W., H. Mentzel, and T. Pieler. 1990. The Xenopus laevis poly(A) binding protein is composed of multiple functionally independent RNA binding domains. EMBO J. 9: 3699-3705.
25. Pandey, N.B. and W.F. Marzluff. 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.
26. Pandey, N.B., J.-H. Sun, and W.F. Marzluff. 1991. Different complexes are formed on the 3′ end of histone mRNA in nuclear and polysomal extracts. Nucleic Acids Res. 19: 5653-5659.
27. Pandey, N.B., A.S. Williams, J.-H. Sun, V.D. Brown, U. Bond, and W.F. Marzluff. 1994. Point mutations in the stem-loop at the 3′ end of mouse histone mRNA reduce expression by reducing the efficiency of 3′ end formation. Mol. Cell. Biol. 14: 1709-1720.
28. Pinol-Roma, S. and G. Dreyfuss. 1992. Shuttling of pre-mRNA binding proteins between nucleus and cytoplasm. Nature 355: 730-732.
29. Schümperli, D. 1986. Cell-cycle regulation of histone gene expression. Cell 45: 571-572.
30. SenGupta, D., B. Zhang, B. Kraemer, P. Prochart, S. Fields, and M. Wickens. 1996. A three-hybrid system to detect RNA-protein interactions in vivo. Proc. Natl. Acad. Sci. 93: 8496-8501.
31. Soldati, D. and D. Schümperli. 1988. Structural and functional characterization of mouse U7 small nuclear RNA active in 3′ processing of histone pre-mRNA. Mol. Cell. Biol. 8: 1518-1524.
32. Stauber, C. and D. Schümperli. 1988. 3′ processing of pre-mRNA plays a major role in proliferation-dependent regulation of histone gene expression. Nucleic Acids Res. 16: 9399-9413.
33. Stauber, C., B. Lüscher, R. Eckner, E. Lotscher, and D. Schümperli. 1986. A signal regulating mouse histone H4 mRNA levels in a mammalian cell cycle mutant and sequences controlling RNA 3′ processing are both contained within the same 80-bp fragment. EMBO J. 5: 3297-3303.
34. Streit, A., T.W. Koning, D. Soldati, L. Melin, and D. Schümperli. 1993. Variable effects of the conserved RNA hairpin element upon 3′ end processing of histone pre-mRNA in vitro. Nucleic Acids Res. 21: 1569-1575.
35. Sun, J.-H., D.R. Pilch, and W.F. Marzluff. 1992. The histone mRNA 3′ end is required for localization of histone mRNA to polyribosomes. Nucleic Acids Res. 20: 6057-6066.
36. Taylor, J.D., S.E. Wellman, and W.F. Marzluff. 1986. Sequences of four mouse histone H3 genes: Implications for evolution of mouse histone genes. J. Mol. Evol. 23: 242-249.
37. Vasserot, A.P., F.J. Schaufele, and M.L. Bimstiel. 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. 86: 4345-4349.
38. Williams, A.S. and W.F. Marzluff. 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.
39. Williams, A.S., T.C. Ingeldue, B.K. Kay, and W.F. Marzluff. 1994. Changes in the stem-loop at the 3′ terminus of histone mRNA affects its nucleocytoplasmic transport and cytoplasmic regulation. Nucleic Acids Res. 22: 4660-4666.