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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 major yeast poly(A)-binding protein is associated with cleavage factor IA and functions in premessenger RNA 3'-end formation.
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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)
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   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.
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Structure-Function Relationships in the Saccharomyces cerevisiae Poly(A) Polymerase.
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The 160-kD subunit of human cleavage-polyadenylation specificity factor coordinates pre-mRNA 3'-end formation..
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