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Sequences similarities have been noted between the 77-kD and the 64-kD subunits of human CstF and yeast Rna14 and Rna15, respectively [Y. Takagaki and J. L. Manley, Nature 372, 471 (1994)]. However, these similarities are not very strong or restricted to an RNA-binding domain.
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note
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A minimal fragment of 2.8 kb complementing the brr5-1 mutant was identified by partial restriction enzyme digestion of the original complementing plasmid. Sequencing this insert revealed a single open reading frame (ORF). We confirmed that this ORF corresponded to Brr5/Ysh1 (and not to a suppressor) by creating a wild-type strain in which the chromosomal version of the gene was marked by URA3. This strain was crossed to a ura3 brr5-1 strain, the diploid was sporulated, and the meiotic progeny were assessed for cold sensitivity (cs) and uracil auxotrophy. Among 18 tetrads, all of the cs spores were also uracil auxotrophs, whereas all cold-resistant spores were uracil prototrophs, indicating linkage of the markers. To determine whether BRR5/YSH1 is essential, we prepared a disrupted version by replacing almost the entire coding sequence with the LEU2 gene. This disrupted allele was used to replace one copy of BRR5/YSH1 in a wild-type diploid strain by homologous recombination. A diploid heterozygous for the BRR5/YSH1 disruption was sporulated, and the resulting ascospores were dissected. Each of the 12 ascii dissected gave rise to only two colonies, both leucine auxotrophs. indicating that BRR5/YSH1 is essential for viability.
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BRR5 was independently cloned and characterized by A. Jenny, L. Minvielle-Sebastia, P. Preker, and W. Keller as similar to the 73-kD subunit of CPSF and named YSH1 (Yeast Seventy-three Homolog 1; personal communication) We adopted the name BRR5/YSH1.
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note
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The total amount of poly(A) RNA was decreased in brr5-1 at the nonpermissive temperature The poly(A) tail lengths in the brr5-1 strain showed no significant difference with the wild type, even at the nonpermissive temperature.
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The disparate effects of brr5-1 on cleavage in vivo and in vitro are reminiscent of previous observations of a Poly(A) polymerase mutant, which affects only polyadenylation in vitro [D. Patel and J. S. Butler, Mol. Cell. Biol. 12, 3297 (1992)], but also affects cleavage site choice in vivo [E. Mandart and R. Parker, ibid. 15, 6579 (1995)]. These observations suggest that the cleavage and polyadenylation steps may be more strictly coupled in vivo than in vitro.
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The disparate effects of brr5-1 on cleavage in vivo and in vitro are reminiscent of previous observations of a Poly(A) polymerase mutant, which affects only polyadenylation in vitro [D. Patel and J. S. Butler, Mol. Cell. Biol. 12, 3297 (1992)], but also affects cleavage site choice in vivo [E. Mandart and R. Parker, ibid. 15, 6579 (1995)]. These observations suggest that the cleavage and polyadenylation steps may be more strictly coupled in vivo than in vitro.
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Mandart, E.1
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Three copies of the hemagglutinin epitope were inserted before the stop codon of the BRR5/YSH1 ORF. The corresponding replicative plasmid carrying a URA3 marker and the epitope-tagged version of BRR5/YSH1 was transformed into the diploid strain heterozygous for the BRR5/YSH1 disruption. The transformants were sporulated, and the resulting ascospores were dissected. Ascospores prototrophic for uracil and leucine were viable, showing that the epitope-tagged version of the gene is able to complement the gene disruption.
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unpublished results
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G. Chanfreau, unpublished results.
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note
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We thank W. Keller and F. Lacroute for antibodies and P. Preker for plasmids and helpful advice; A. Gamarnik and R. Andino for help with FPLC; A. Jenny, L. Minvielle-Sebastia, P. Preker, and W. Keller for communication of unpublished results; L. Esperas, C. Pudlow, and H. Roiha for technical assistance; A. Frankel, E. O'Shea, C. Siebel, and J. Staley for critical reading of the manuscript; H. Madhani for noting the Synechocystis bfh sequence and major help with the manuscript; and members of the Guthrie laboratory for sharing experimental expertise. Supported by NIH grant GM21119 (C.G.), a Human Frontier Science Program long-term postdoctoral fellowship (G.C.), and an American Heart Association Predoctoral Fellowship (S.N.). C.G. is an American Cancer Society Research Professor of Molecular Genetics.
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