Mutations in the RNA binding domain of stem-loop binding protein define separable requirements for RNA binding and for histone pre-mRNA processing

Molecular and Cellular Biology

Volumn 21, Issue 6, 2001, Pages 2008-2017

  Dominski, Zbigniew ^a   Erkmann, Judith A ^a   Greenland, John A ^a   Marzluff, William F ^a,b  

^a UNIVERSITY OF NORTH CAROLINA SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF NORTH CAROLINA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; HISTONE; MESSENGER RNA PRECURSOR; RNA; SMALL NUCLEAR RIBONUCLEOPROTEIN; STEM LOOP BINDING PROTEIN; TYROSINE; UNCLASSIFIED DRUG;

3' UNTRANSLATED REGION; AMINO ACID SEQUENCE; ARTICLE; CONTROLLED STUDY; GENE EXPRESSION; MOLECULAR RECOGNITION; MUTATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; RNA BINDING; RNA PROCESSING; SEQUENCE ANALYSIS; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CONSERVED SEQUENCE; GENETIC COMPLEMENTATION TEST; HISTONES; HUMANS; MOLECULAR SEQUENCE DATA; MRNA CLEAVAGE AND POLYADENYLATION FACTORS; MUTATION; NUCLEAR PROTEINS; RIBONUCLEOPROTEIN, U7 SMALL NUCLEAR; RNA PRECURSORS; RNA PROCESSING, POST-TRANSCRIPTIONAL; RNA, MESSENGER; RNA-BINDING PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; XENOPUS; XENOPUS PROTEINS;

EID: 0035019667     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.21.6.2008-2017.2001     Document Type: Article

References (33)

1. Calnan, B. J., S. Biancalana, D. Hudson, and A. D. Frankel. 1991. Analysis of arginine-rich peptides from the HIV Tat protein reveals unusual features of RNA-protein recognition. Genes Dev. 5:201-210.
2. Gotten, 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.
3. Dominski, Z., and W. F. Marzluff. 1999. Formation of the 3′ end of histone mRNA. Gene 239:1-14.
4. 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.
5. Dominski, Z., L.-X. Zheng, R. Sanchez, and W. F. Marzluff. 1999 The stem-loop binding protein facilitates 3′ end formation by stabilizing U7 snRNP binding to the histone pre-mRNA. Mol. Cell. Biol. 19:3561-3570.
6. Galli, G., H. Hofstetter, H. G. Stunnenberg, and M. L. Birnstiel. 1983. Biochemical complementation with RNA in the Xenopus oocyte: a small RNA is required for the generation of 3′ histone mRNA termini. Cell 34:823-828.
7. Gallic, D. R., N. J. Lewis, and W. F. Marzluff. 1996. The histone 3′-terminal stem-loop is necessary for translation in Chinese hamster ovary cells. Nucleic Acids Res. 24:1954-1962.
8. Gick, O., A. Krämer, W. Keller, and M. L. Birnstiel. 1986. Generation of histone mRNA 3′ ends by endonucleolytic cleavage of the pre-mRNA in a snRNP-dependent in vitro reaction. EMBO J. 5:1319-1326.
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. USA 84:8937-8940.
10. 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.
11. Ingledue, T. C., Z. Dominski, R. Sanchez, J. A. Erkmann, and W. F. Marzluff. 2000. Dual role for the RNA-binding domain of Xenopus laevis SLBP1 in histone pre-mRNA processing. RNA 6:1635-1648.
12. Krieg, P. A., and D. A. Melton. 1984. Formation of the 3′ end of histone mRNA by post-transcriptional processing. Nature 308:203-206.
13. Martin, F., F. Michel, D. Zenklusen, B. Müller, and D. Schümperli. 2000. Positive and negative mutant selection in the human histone hairpin-binding protein using the yeast three-hybrid system. Nucleic Acids Res. 28:1594-1603.
14. Martin, F., A. Schaller, S. Eglite, D. Schümperli, and B. Müller. 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. 16: 769-778.
15. Marzluff, W. F. 1992. Histone 3′ ends: essential and regulatory functions. Gene Expr. 2:93-97.
16. Marzluff, W. F., M. L. Whitfield, Z. Dominski, and Z.-F. Wang. 1997. Identification of the protein that interacts with the 3′ end of histone mRNA, p. 163-193. In J. D. Richter (ed.), mRNA formation and function. Academic Press, New York, N.Y.
17. 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.
18. Mowry, K. L., and J. A. Steitz. 1987. 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.
19. 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.
20. Smith, H. O., K. Tabiti, G. Schaffner, D. Soldati, U. Albrecht, and M. L. Birnstiel. 1991. Two-step affinity purification of U7 small nuclear ribonucleoprotein particles using complementary biotinylated 2′-O-methyl oligoribonucleotides. Proc. Natl. Acad. Sci. USA 88:9784-9788.
21. Spycher, C., A. Streit, B. Stefanovic, D. Albrecht, T. H. W. Koning, and D. Schümperli. 1994. 3′ end processing of mouse histone pre-mRNA: evidence for additional base-pairing between U7 snRNA and pre-mRNA. Nucleic Acids Res. 22:4023-4030.
22. Stefanovic, B., W. Hackl, R. Lührmann, and D. Schümperli. 1995. Assembly, nuclear import and function of U7 snRNPs studied by microinjection of synthetic U7 RNA into Xenopus oocytes. Nucleic Acids Res. 23:3141-3151.
23. Streit, A., T. W. Koning, D. Soldati, L. Melin, and D. Schümperli. 1993. Variable effects of the conserved RNA hairpin clement upon 3′ end processing of histone pre-mRNA in vitro. Nucleic Acids Res. 21:1569-1575.
24. Sullivan, E., C. Santiago, E. D. Parker, Z. Dominski, X. Yang, D. J. Lanzotti, T. C. Ingledue, W. F. Marzluff, and R. J. Duronio. 2001. Drosophila stem loop binding protein coordinates accumulation of mature histone mRNA with cell cycle progression. Genes Dev. 15:173-181.
25. 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.
26. Varani, G., and K. Nagai. 1998. RNA recognition by RNP proteins during RNA processing. Annu. Rev. Biophys. Biomol. Struct. 27:407-445.
27. Vasserot, A. P., F. J. Schaufele, and M. L. Birnstiel. 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.
28. Wang, Z.-F., T. C. Ingledue, Z. Dominski, R. Sanchez, and W. F. Marzluff. 1999. Two Xenopus proteins that bind the 3′ end of histone mRNA: implications for translational control of histone synthesis during oogenesis. Mol. Cell. Biol. 19:835-845.
29. Wang, Z.-K., M. L. Whitfield, T. I. Ingledue, Z. Dominski, and W. F. Marzluff. 1996. The protein which binds the 3′ end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing. Genes Dev. 10:3028-3040.
30. Whitfield, M. L., L.-X. Zheng, A. Baldwin, T. Ohta, M. M. Hurt, and W. F. Marzluff. 2000. Stem-loop binding protein, the protein that binds the 3′ end of histone mRNA, is cell cycle regulated by both translational and posttranslational mechanisms. Mol. Cell. Biol. 20:4188-4198.
31. Williams, A. S., T. C. Ingledue, 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.
32. 35. Nature 402:832-835.
33. Zorin, D. A. R., and T. Blumenthal. 1999. Both subunits of U2AF recognize the 3′ splice site in Caenorhabditis elegans. Nature 402:835-838.