Stimulatory effect of splicing factors on transcriptional elongation (original) (raw)

• Bentley, D. Coupling RNA polymerase II transcription with pre-mRNA processing. Curr. Opin. Cell Biol. 11, 347–351 (1999).
  Article CAS Google Scholar
• Hirose, Y. & Manley, J. L. RNA polymerase II and the integration of nuclear events. Genes Dev. 14, 1415–1429 (2000).
  CAS PubMed Google Scholar
• McCracken, S. et al. The C-terminal domain of RNA polymerase II couples mRNA processing to transcription. Nature 385, 357–361 (1997).
  Article ADS CAS Google Scholar
• Fong, N. & Bentley, D. L. Capping, splicing, and 3′ processing are independently stimulated by RNA polymerase II: different functions for different segments of the CTD. Genes Dev. 15, 1783–1795 (2001).
  Article CAS Google Scholar
• Hirose, Y., Tacke, R. & Manley, J. L. Phosphorylated RNA polymerase II stimulates pre-mRNA splicing. Genes Dev. 13, 1234–1239 (1999).
  Article CAS Google Scholar
• Kim, J. B., Yamaguchi, Y., Wada, T., Handa, H. & Sharp, P. A. Tat-SF1 protein associates with RAP30 and human SPT5 proteins. Mol. Cell. Biol. 19, 5960–5968 (1999).
  Article CAS Google Scholar
• Li, X. Y. & Green, M. R. The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor. Genes Dev. 12, 2992–2996 (1998).
  Article CAS Google Scholar
• Zhou, Q. & Sharp, P. A. Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. Science 274, 605–610 (1996).
  Article ADS CAS Google Scholar
• Parada, C. A. & Roeder, R. G. A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription. EMBO J. 18, 3688–3701 (1999).
  Article CAS Google Scholar
• Price, D. H. P-TEFb, a cyclin-dependent kinase controlling elongation by RNA polymerase II. Mol. Cell. Biol. 20, 2629–2634 (2000).
  Article CAS Google Scholar
• Ping, Y. H. & Rana, T. M. Tat-associated kinase (P-TEFb): a component of transcription preinitiation and elongation complexes. J. Biol. Chem. 274, 7399–7404 (1999).
  Article CAS Google Scholar
• Zhou, M. et al. Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription. Mol. Cell. Biol. 20, 5077–5086 (2000).
  Article CAS Google Scholar
• Dahmus, M. E. Reversible phosphorylation of the C-terminal domain of RNA polymerase II. J. Biol. Chem. 271, 19009–19012 (1996).
  Article CAS Google Scholar
• Wei, P., Garber, M. E., Fang, S. M., Fischer, W. H. & Jones, K. A. A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA. Cell 92, 451–462 (1998).
  Article CAS Google Scholar
• Jones, K. A. Taking a new TAK on tat transactivation. Genes Dev. 11, 2593–2599 (1997).
  Article CAS Google Scholar
• Garber, M. E. et al. The interaction between HIV-1 Tat and human cyclin T1 requires zinc and a critical cysteine residue that is not conserved in the murine CycT1 protein. Genes Dev. 12, 3512–3527 (1998).
  Article CAS Google Scholar
• Peng, J., Zhu, Y., Milton, J. T. & Price, D. H. Identification of multiple cyclin subunits of human P-TEFb. Genes Dev. 12, 755–762 (1998).
  Article CAS Google Scholar
• Fong, Y. W. & Zhou, Q. Relief of two built-in autoinhibitory mechanisms in P-TEFb is required for assembly of a multicomponent transcription elongation complex at the human immunodeficiency virus type 1 promoter. Mol. Cell. Biol. 20, 5897–5907 (2000).
  Article CAS Google Scholar
• Zhou, Q. & Sharp, P. A. Novel mechanism and factor for regulation by HIV-1 Tat. EMBO J. 14, 321–328 (1995).
  Article CAS Google Scholar
• Marciniak, R. A. & Sharp, P. A. HIV-1 Tat protein promotes formation of more-processive elongation complexes. EMBO J. 10, 4189–4196 (1991).
  Article CAS Google Scholar
• Yan, D. et al. CUS2, a yeast homolog of human Tat-SF1, rescues function of misfolded U2 through an unusual RNA recognition motif. Mol. Cell. Biol. 18, 5000–5009 (1998).
  Article CAS Google Scholar
• Perriman, R. & Ares, M. Jr ATP can be dispensable for prespliceosome formation in yeast. Genes Dev. 14, 97–107 (2000).
  CAS PubMed PubMed Central Google Scholar
• Krainer, A. R. Pre-mRNA splicing by complementation with purified human U1, U2, U4/U6 and U5 snRNPs. Nucleic Acids Res. 16, 9415–9429 (1988).
  Article CAS Google Scholar
• Bach, M., Bringmann, P. & Lührmann, R. Purification of small nuclear ribonucleoprotein particles with antibodies against modified nucleosides of small nuclear RNAs. Methods Enzymol. 181, 232–257 (1990).
  Article CAS Google Scholar
• Blencowe, B. J. & Lamond, A. I. Purification and depletion of RNP particles by antisense affinity chromatography. Methods Mol. Biol. 118, 275–287 (1999).
  CAS PubMed Google Scholar
• Schnapp, G., Rodi, H. P., Rettig, W. J., Schnapp, A. & Damm, K. One-step affinity purification protocol for human telomerase. Nucleic Acids Res. 26, 3311–3313 (1998).
  Article CAS Google Scholar
• Krainer, A. R. & Maniatis, T. Multiple factors including the small nuclear ribonucleoproteins U1 and U2 are necessary for pre-mRNA splicing in vitro. Cell 42, 725–736 (1985).
  Article CAS Google Scholar
• Solnick, D. Alternative splicing caused by RNA secondary structure. Cell 43, 667–676 (1985).
  Article CAS Google Scholar
• Padgett, R. A., Mount, S. M., Steitz, J. A. & Sharp, P. A. Splicing of messenger RNA precursors is inhibited by antisera to small nuclear ribonucleoprotein. Cell 35, 101–107 (1983).
  Article CAS Google Scholar
• Ares, M. Jr, Grate, L. & Pauling, M. H. A handful of intron-containing genes produces the lion's share of yeast mRNA. RNA 9, 1138–1139 (1999).
  Article Google Scholar