MRNA polyadenylation and its coupling to other RNA processing reactions and to transcription

Current Opinion in Cell Biology

Volumn 11, Issue 3, 1999, Pages 352-357

  Minvielle Sebastia, Lionel ^a   Keller, Walter ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

MESSENGER RNA;

MESSENGER RNA SYNTHESIS; POLYADENYLATION; PRIORITY JOURNAL; QUALITY CONTROL; REVIEW; RNA CAPPING; RNA PROCESSING; RNA SPLICING; RNA TRANSCRIPTION; SACCHAROMYCES CEREVISIAE; VERTEBRATE;

EUKARYOTA; SACCHAROMYCES CEREVISIAE; VERTEBRATA;

EID: 0033151767     PISSN: 09550674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0955-0674(99)80049-0     Document Type: Review

References (52)

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29. Nemeroff ME, Barabino SML, Li Y, Keller W, Krug RM: Influenza virus NS1 protein interacts with the cellular 30 kDa subunit of CPSF and inhibits 3′end formation of cellular pre-mRNAs. Mol Cell 1998, 1:991-1000. This study shows that the influenza A virus NS1 protein inhibits the export of the host cell mRNAs. It directly interacts with CPSF-30K which prevents pre-mRNA 3′-end processing.
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40. Bauren G, Belikov S, Wieslander L: Transcriptional termination in the Balbiani ring 1 gene is closely coupled to 3′-end formation and excision of the 3′-terminal intron. Genes Dev 1998, 12:2759-2769.
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42. Birse CE, Minvielle-Sebastia L, Lee BA, Keller W, Proudfoot NJ: Cleavage of the primary transcript couples 3′-end RNA-processing with termination of pol II transcription. Science 1998, 280:298-301. This study demonstrates that efficient termination of transcription requires a functional cleavage activity in yeast. Polyadenylation mutants do not seem to affect pol II termination. These results show that the coupling of 3′ processing and transcription requires efficient cleavage of the pre-mRNA.
43. McCracken S, Fong N, Yankulov K, Ballantyne S, Pan G, Greenblatt J, Patterson SD, Wickens M, Bentley DL: The C-terminal domain of RNA polymerase II couples mRNA processing to transcription. Nature 1997, 385:357-361. The four papers [43••-46••] show direct interactions of pre-mRNA processing factors with the RNA polymerase II carboxy-terminal domain (CTD). This paper was the first to show that CPSF and CstF are found associated with the CTD of pol II, providing insights into the mechanism of coupling between polyadenylation and transcription.
44. McCracken S, Fong N, Rosonina E, Yankulov K, Brothers G, Siderovski D, Hessel A, Foster S, Shuman S, Bentley DL: 5′-capping enzymes are targeted to pre-mRNA by binding to the phosphorylated carboxy-terminal domain of RNA polymerase II. Genes Dev 1997, 11:3306-3318. The association of the capping enzymes with the phosphorylated CTD of pol II is required for efficient pre-mRNA capping. This study and [45••] arrive at the same conclusions.
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50. 0 to S phase transition. Proc Natl Acad Sci USA 1998, 95:11095-11100. In contradiction to [49•], the authors show that the CstF-64K levels can change no matter whether the B cells differentiate or not. As variation of the CstF-64K concentration is not correlated with the production of the secretory-specific IgM mRNA, they suggest that another factor is required.
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