Phosphorylation of Stem-Loop Binding Protein (SLBP) on Two Threonines Triggers Degradation of SLBP, the Sole Cell Cycle-Regulated Factor Required for Regulation of Histone mRNA Processing, at the End of S Phase

REFERENCES

• Adam, M., F. Robert, M. Larochelle, and L. Gaudreau. 2001. H2A.Z is required for global chromatin integrity and for recruitment of RNA polymerase II under specific conditions. Mol. Cell. Biol. 21: 6270–6279.
   PubMed Web of Science ®Google Scholar
• Ahmad, K., and S. Henikoff. 2002. The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly. Mol. Cell 9: 1191–1200.
   PubMed Web of Science ®Google Scholar
• Birchmeier, C., W. Folk, and M. L. Birnstiel. 1983. The terminal RNA stem-loop structure and 80 bp of spacer DNA are required for the formation of 3′ termini of sea urchin H2A mRNA. Cell 35: 433–440.
   PubMedGoogle Scholar
• Bond, G. L., C. Prives, and J. L. Manley. 2000. Poly(A) polymerase phosphorylation is dependent on novel interactions with cyclins. Mol. Cell. Biol. 20: 5310–5320.
   PubMedGoogle Scholar
• Brandeis, M., and T. Hunt. 1996. The proteolysis of mitotic cyclins in mammalian cells persists from the end of mitosis until the onset of S phase. EMBO J. 15: 5280–5289.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• DeLisle, A. J., R. A. Graves, W. F. Marzluff, and L. F. Johnson. 1983. Regulation of histone mRNA production and stability in serum-stimulated mouse fibroblasts. Mol. Cell. Biol. 3: 1920–1929.
   PubMed Web of Science ®Google Scholar
• Dominski, Z., and W. F. Marzluff. 1999. Formation of the 3′ end of histone mRNA. Gene 239: 1–14.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Fan, J. Y., F. Gordon, K. Luger, J. C. Hansen, and D. J. Tremethick. 2002. The essential histone variant H2A.Z regulates the equilibrium between different chromatin conformational states. Nat. Struct. Biol. 9: 172–176.
   PubMedGoogle Scholar
• Feldman, R. M., C. C. Correll, K. B. Kaplan, and R. J. Deshaies. 1997. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91: 221–230.
   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 cleavage of the pre-mRNA in a snRNP-dependent in vitro reaction. EMBO J. 5: 1319–1326.
   PubMedGoogle Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Hall, C., D. M. Nelson, X. F. Ye, K. Baker, J. A. DeCaprio, S. Seeholzer, M. Lipinski, and P. D. Adams. 2001. HIRA, the human homologue of yeast Hir1p and Hir2p, is a novel cyclin-cdk2 substrate whose expression blocks S-phase progression. Mol. Cell. Biol. 21: 1854–1865.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• Harris, M. E., R. Bühni, 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.
   PubMed Web of Science ®Google Scholar
• Heintz, N., H. L. Sive, and R. G. Roeder. 1983. Regulation of human histone gene expression: kinetics of accumulation and changes in the rate of synthesis and in the half-lives of individual histone mRNAs during the HeLa cell cycle. Mol. Cell. Biol. 3: 539–550.
   PubMed Web of Science ®Google Scholar
• Henikoff, S., K. Ahmad, J. S. Platero, and B. Van Steensel. 2000. Heterochromatic deposition of centromeric histone H3-like proteins. Proc. Natl. Acad. Sci. USA 97: 716–721.
   PubMedGoogle Scholar
• Hoffmann, I., and M. L. Birnstiel. 1990. Cell cycle-dependent regulation of histone precursor mRNA processing by modulation of U7 snRNA accessibility. Nature 346: 665–668.
   PubMedGoogle Scholar
• Jackson, J. D., and M. A. Gorovsky. 2000. Histone H2A.Z has a conserved function that is distinct from that of the major H2A sequence variants. Nucleic Acids Res. 28: 3811–3816.
   PubMed Web of Science ®Google Scholar
• Koepp, D. M., L. K. Schaefer, X. Ye, K. Keyomarsi, C. Chu, J. W. Harper, and S. J. Elledge. 2001. Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase. Science 294: 173–177.
   PubMed Web of Science ®Google Scholar
• Lüscher, B., and D. Schümperli. 1987. RNA 3′ processing regulates histone mRNA levels in a mammalian cell mutant. A processing factor becomes limiting in G1-arrested cells. EMBO J. 6: 1721–1726.
   PubMedGoogle Scholar
• 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.
   PubMedGoogle Scholar
• Marzluff, W. F. 1992. Histone 3′ ends: essential and regulatory functions. Gene Expr. 2: 93–97.
   PubMedGoogle Scholar
• Marzluff, W. F., and R. J. Duronio. 2002. Histone mRNA expression: multiple levels of cell cycle regulation and important developmental consequences. Curr. Opin. Cell Biol. 14: 692–699.
   PubMed Web of Science ®Google Scholar
• 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.
   Google Scholar
• Michael, W. M., and J. Newport. 1998. Coupling of mitosis to the completion of S phase through Cdc34-mediated degradation of Wee1. Science 282: 1886–1889.
   PubMedGoogle Scholar
• Moberg, K. H., D. W. Bell, D. C. R. Wahrer, D. A. Haber, and I. K. Hariharan. 2001. Archipelago regulates cyclin E levels in Drosophila and is mutated in human cancer cell lines. Nature 413: 311–316.
   PubMed Web of Science ®Google Scholar
• Morgan, D. O. 1999. Regulation of the APC and the exit from mitosis. Nat. Cell Biol. 1: E47–E53.
   PubMedGoogle Scholar
• Mowry, K. L., and J. A. Steitz. 1987. 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• Pagano, M., S. W. Tam, A. M. Theodoras, P. Beer-Romero, G. Del Sal, V. Chau, P. R. Yew, G. F. Draetta, and M. Rolfe. 1995. Role of the ubiquitin-proteasome pathway in regulating abundance of the cyclin-dependent kinase inhibitor p27. Science 269: 682–685.
   PubMed Web of Science ®Google Scholar
• Paull, T. T., E. P. Rogakou, V. Yamazaki, C. U. Kirchgessner, M. Gellert, and W. M. Bonner. 2000. A critical role for histone H2AX in recruitment of repair factors to nuclear foci after DNA damage. Curr. Biol. 10: 886–895.
   PubMed Web of Science ®Google Scholar
• Redon, C., D. Pilch, E. Rogakou, O. Sedelnikova, K. Newrock, and W. Bonner. 2002. Histone H2A variants H2AX and H2AZ. Curr. Opin. Genet. Dev. 12: 162–169.
   PubMed Web of Science ®Google Scholar
• Russo, A. A., P. D. Jeffrey, A. K. Patten, J. Massagué, and N. P. Pavletich. 1996. Crystal structure of the p27Kip1 cyclin-dependent-kinase inhibitor bound to the cyclin A Cdk2 complex. Nature 382: 325–331.
   PubMed Web of Science ®Google Scholar
• Sanchez, R., and W. F. Marzluff. 2002. The stem-loop binding protein is required for efficient translation of histone mRNA in vivo and in vitro. Mol. Cell. Biol. 22: 7093–7104.
   PubMed Web of Science ®Google Scholar
• Schulman, B. A., D. L. Lindstrom, and E. Harlow. 1998. Substrate recruitment to cyclin-dependent kinase 2 by a multipurpose docking site on cyclin A. Proc. Natl. Acad. Sci. USA 95: 10453–10458.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Strohmaier, H., C. H. Spruck, P. Kaiser, K. A. Won, O. Sangfelt, and S. I. Reed. 2001. Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413: 316–322.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMedGoogle Scholar
• Wang, Z.-F., 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.
   PubMed Web of Science ®Google Scholar
• 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.
   PubMed Web of Science ®Google Scholar