RNA polymerase II is an essential mRNA polyadenylation factor - PubMed (original) (raw)
. 1998 Sep 3;395(6697):93-6.
doi: 10.1038/25786.
Affiliations
- PMID: 9738505
- DOI: 10.1038/25786
RNA polymerase II is an essential mRNA polyadenylation factor
Y Hirose et al. Nature. 1998.
Abstract
Production of messenger RNA in eukaryotic cells is a complex, multistep process. mRNA polyadenylation, or 3' processing, requires several protein factors, including cleavage/polyadenylation-specificity factor (CPSF), cleavage-stimulation factor, two cleavage factors and poly(A) polymerase. These proteins seem to be unnecessary for other steps in mRNA synthesis such as transcription and splicing, and factors required for these processes were not considered to be essential for polyadenylation. Nonetheless, these reactions may be linked so that they are effectively coordinated in vivo. For example, the CTD carboxy-terminal domain of the largest subunit of RNA polymerase II (RNAP II) is required for efficient splicing and polyadenylation in vivo, and CPSF is brought to a promoter by the transcription factor TFIID and transferred to RNAP II at the time of transcription initiation. These findings suggest that polyadenylation factors can be recruited to an RNA 3'-processing signal by RNAP II, where they dissociate from the polymerase and initiate polyadenylation. Here we present results that extend this model by showing that RNAP II is actually required, in the absence of transcription, for 3' processing in vitro.
Comment in
- RNA processing. A tale of two tails.
Bentley D. Bentley D. Nature. 1998 Sep 3;395(6697):21-2. doi: 10.1038/25616. Nature. 1998. PMID: 9738492 No abstract available.
Similar articles
- The C-terminal domain of RNA polymerase II couples mRNA processing to transcription.
McCracken S, Fong N, Yankulov K, Ballantyne S, Pan G, Greenblatt J, Patterson SD, Wickens M, Bentley DL. McCracken S, et al. Nature. 1997 Jan 23;385(6614):357-61. doi: 10.1038/385357a0. Nature. 1997. PMID: 9002523 - Transcription factor TFIID recruits factor CPSF for formation of 3' end of mRNA.
Dantonel JC, Murthy KG, Manley JL, Tora L. Dantonel JC, et al. Nature. 1997 Sep 25;389(6649):399-402. doi: 10.1038/38763. Nature. 1997. PMID: 9311784 - The yeast Rat1 exonuclease promotes transcription termination by RNA polymerase II.
Kim M, Krogan NJ, Vasiljeva L, Rando OJ, Nedea E, Greenblatt JF, Buratowski S. Kim M, et al. Nature. 2004 Nov 25;432(7016):517-22. doi: 10.1038/nature03041. Nature. 2004. PMID: 15565157 - mRNA polyadenylation and its coupling to other RNA processing reactions and to transcription.
Minvielle-Sebastia L, Keller W. Minvielle-Sebastia L, et al. Curr Opin Cell Biol. 1999 Jun;11(3):352-7. doi: 10.1016/S0955-0674(99)80049-0. Curr Opin Cell Biol. 1999. PMID: 10395555 Review. - [C-terminal domain (CTD) of the subunit Rpb1 of nuclear RNA polymerase II and its role in the transcription cycle].
Sobennikova MV, Shematorova EK, Shpakovskiĭ GV. Sobennikova MV, et al. Mol Biol (Mosk). 2007 May-Jun;41(3):433-49. Mol Biol (Mosk). 2007. PMID: 17685222 Review. Russian.
Cited by
- Nuclear deadenylation/polyadenylation factors regulate 3' processing in response to DNA damage.
Cevher MA, Zhang X, Fernandez S, Kim S, Baquero J, Nilsson P, Lee S, Virtanen A, Kleiman FE. Cevher MA, et al. EMBO J. 2010 May 19;29(10):1674-87. doi: 10.1038/emboj.2010.59. Epub 2010 Apr 8. EMBO J. 2010. PMID: 20379136 Free PMC article. - Transcription-independent RNA polymerase II dephosphorylation by the FCP1 carboxy-terminal domain phosphatase in Xenopus laevis early embryos.
Palancade B, Dubois MF, Dahmus ME, Bensaude O. Palancade B, et al. Mol Cell Biol. 2001 Oct;21(19):6359-68. doi: 10.1128/MCB.21.19.6359-6368.2001. Mol Cell Biol. 2001. PMID: 11533226 Free PMC article. - Polyadenylation of rRNA- and tRNA-based yeast transcripts cleaved by internal ribozyme activity.
Düvel K, Pries R, Braus GH. Düvel K, et al. Curr Genet. 2003 Jul;43(4):255-62. doi: 10.1007/s00294-003-0401-8. Epub 2003 May 14. Curr Genet. 2003. PMID: 12748813 - Kin28, the TFIIH-associated carboxy-terminal domain kinase, facilitates the recruitment of mRNA processing machinery to RNA polymerase II.
Rodriguez CR, Cho EJ, Keogh MC, Moore CL, Greenleaf AL, Buratowski S. Rodriguez CR, et al. Mol Cell Biol. 2000 Jan;20(1):104-12. doi: 10.1128/MCB.20.1.104-112.2000. Mol Cell Biol. 2000. PMID: 10594013 Free PMC article. - Heterogeneity in mammalian RNA 3' end formation.
Neilson JR, Sandberg R. Neilson JR, et al. Exp Cell Res. 2010 May 1;316(8):1357-64. doi: 10.1016/j.yexcr.2010.02.040. Epub 2010 Mar 6. Exp Cell Res. 2010. PMID: 20211174 Free PMC article. Review.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources