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Science 9 December 1994:
Vol. 266. no. 5191, pp. 1702 - 1705
DOI: 10.1126/science.7992054
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Articles

Science, Vol 266, Issue 5191, 1702-1705
Copyright © 1994 by American Association for the Advancement of Science

articles

RNA14 and RNA15 proteins as components of a yeast pre-mRNA 3'-end processing factor

L Minvielle-Sebastia, PJ Preker, and W Keller

Department of Cell Biology, University of Basel, Switzerland.

Most eukaryotic pre-messenger RNAs are processed at their 3' ends by endonucleolytic cleavage and polyadenylation. In yeast, this processing requires polyadenylate [poly(A)] polymerase (PAP) and other proteins that have not yet been characterized. Here, mutations in the PAP1 gene were shown to be synergistically lethal with previously identified mutations in the RNA14 and RNA15 genes, which suggests that their encoded proteins participate in 3'-end processing. Indeed, extracts from ma14 and rna15 mutants were shown to be deficient in both steps of processing. Biochemical complementation experiments and reconstitution of both activities with partially purified cleavage factor I (CF I) validated the genetic prediction.


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The structure of the CstF-77 homodimer provides insights into CstF assembly.
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Depletion of the Yeast Nuclear Exosome Subunit Rrp6 Results in Accumulation of Polyadenylated RNAs in a Discrete Domain within the Nucleolus.
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The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3'-end formation.
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Functional Analysis of Yeast snoRNA and snRNA 3'-End Formation Mediated by Uncoupling of Cleavage and Polyadenylation.
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Kin28, the TFIIH-Associated Carboxy-Terminal Domain Kinase, Facilitates the Recruitment of mRNA Processing Machinery to RNA Polymerase II.
C. R. Rodriguez, E.-J. Cho, M.-C. Keogh, C. L. Moore, A. L. Greenleaf, and S. Buratowski (2000)
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Posttranscriptional Control of Gene Expression in Yeast.
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Poly(A) Tail Length Control in Saccharomyces cerevisiae Occurs by Message-Specific Deadenylation.
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The upstream sequence element of the C2 complement poly(A) signal activates mRNA 3' end formation by two distinct mechanisms.
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Coupling Termination of Transcription to Messenger RNA Maturation in Yeast.
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Mechanism and regulation of mRNA polyadenylation.
D. F. Colgan and J. L. Manley (1997)
Genes & Dev. 11, 2755-2766
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Alternative 3'-end processing of U5 snRNA by RNase III.
G. Chanfreau, S. A. Elela, M. Ares Jr., and C. Guthrie (1997)
Genes & Dev. 11, 2741-2751
   Abstract »    Full Text »    PDF »
The major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3'-end formation.
L. Minvielle-Sebastia, P. J. Preker, T. Wiederkehr, Y. Strahm, and W. Keller (1997)
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   Abstract »    Full Text »    PDF »
The 30-kD subunit of mammalian cleavage and polyadenylation specificity factor and its yeast homolog are RNA-binding zinc finger proteins..
S M Barabino, W Hubner, A Jenny, L Minvielle-Sebastia, and W Keller (1997)
Genes & Dev. 11, 1703-1716
   Abstract »    PDF »
Cleavage Factor II of Saccharomyces cerevisiae Contains Homologues to Subunits of the Mammalian Cleavage/ Polyadenylation Specificity Factor and Exhibits Sequence-specific, ATP-dependent Interaction with Precursor RNA.
J. Zhao, M. M. Kessler, and C. L. Moore (1997)
J. Biol. Chem. 272, 10831-10838
   Abstract »    Full Text »    PDF »
Structure-Function Relationships in the Saccharomyces cerevisiae Poly(A) Polymerase.
A. M. Zhelkovsky, M. M. Kessler, and C. L. Moore (1995)
J. Biol. Chem. 270, 26715-26720
   Abstract »    Full Text »    PDF »
The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation..
K G Murthy and J L Manley (1995)
Genes & Dev. 9, 2672-2683
   Abstract »    PDF »
An Essential Yeast Gene Encoding a Homolog of Ubiquitin-activating Enzyme.
R. J. Dohmen, R. Stappen, J. P. McGrath, H. Forrov, J. Kolarov, A. Goffeau, and A. Varshavsky (1995)
J. Biol. Chem. 270, 18099-18109
   Abstract »    Full Text »    PDF »
Cleavage/polyadenylation factor IA associates with the carboxyl-terminal domain of RNA polymerase II in Saccharomycescerevisiae.
D. Barilla, B. A. Lee, and N. J. Proudfoot (2001)
PNAS 98, 445-450
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Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I.
S. Gross and C. Moore (2001)
PNAS 98, 6080-6085
   Abstract »    Full Text »    PDF »


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