Sequence similarity between the 73-kilodalton protein of mammalian CPSF and a subunit of yeast polyadenylation factor I

Science

Volumn 274, Issue 5292, 1996, Pages 1514-1517

  Jenny, Andreas ^a,b   Minvielle Sebastia, Lionel ^a   Preker, Pascal J ^a   Keller, Walter ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b EUROPEAN MOLECULAR BIOLOGY LABORATORY   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

CLEAVAGE AND POLYADENYLATION SPECIFICITY FACTOR; COMPLEMENTARY DNA; FUNGAL PROTEIN; MESSENGER RNA; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; PROTEIN SUBUNIT; TRANS ACTING FACTOR;

AMINO ACID SEQUENCE; ARTICLE; IMMUNOPRECIPITATION; MAMMAL; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NORTHERN BLOTTING; POLYADENYLATION; PRIORITY JOURNAL; RNA CLEAVAGE; RNA PROCESSING; SEQUENCE ANALYSIS; SEQUENCE HOMOLOGY; YEAST;

AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CLONING, MOLECULAR; EVOLUTION, MOLECULAR; FUNGAL PROTEINS; HUMANS; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; MRNA CLEAVAGE AND POLYADENYLATION FACTORS; POLY A; POLYNUCLEOTIDE ADENYLYLTRANSFERASE; RNA PRECURSORS; RNA PROCESSING, POST-TRANSCRIPTIONAL; RNA, FUNGAL; RNA, MESSENGER; RNA-BINDING PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

EUKARYOTA; MAMMALIA;

EID: 0029852510     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.274.5292.1514     Document Type: Article

References (36)

1. E. Wahle and W. Keller, Trends Biochem. Sci. 21, 247 (1996); J. L. Manley, Curr. Opin. Genet. Dev. 5, 222 (1995).
2. E. Wahle and W. Keller, Trends Biochem. Sci. 21, 247 (1996); J. L. Manley, Curr. Opin. Genet. Dev. 5, 222 (1995).
3. S. Bienroth, W. Keller, E. Wahle, EMBO J. 12, 585 (1993); E. Wahle, Cell 66, 759 (1991).
4. S. Bienroth, W. Keller, E. Wahle, EMBO J. 12, 585 (1993); E. Wahle, Cell 66, 759 (1991).
5. U. Rüegsegger, K. Beyer, W. Keller, J. Biol. Chem. 271, 6107 (1996); Y. Takagaki, L. C. Ryner, J. L. Manley, Genes Dev. 3, 1711 (1989).
6. U. Rüegsegger, K. Beyer, W. Keller, J. Biol. Chem. 271, 6107 (1996); Y. Takagaki, L. C. Ryner, J. L. Manley, Genes Dev. 3, 1711 (1989).
7. Z. Guo and F. Sherman, Mol. Cell. Biol. 15, 5983 (1995).
8. J. Chen and C. Moore, ibid. 12, 3470 (1992); L. Minvielle-Sebastia, P. J. Preker, W. Keller, Science 266, 1702 (1994).
9. J. Chen and C. Moore, ibid. 12, 3470 (1992); L. Minvielle-Sebastia, P. J. Preker, W. Keller, Science 266, 1702 (1994).
10. Y. Takagaki and J. L. Manley, Nature 372, 471 (1994).
11. S. Bienroth, E. Wahle, C. Suter-Crazzolara, W. Keller, J. Biol. Chem. 266, 19768 (1991); A. Jenny, H.-P. Hauri, W. Keller. Mol. Cell. Biol. 14, 8183 (1994); A. Jenny and W. Keller, Nucleic Acids Res. 23, 2629 (1995).
12. S. Bienroth, E. Wahle, C. Suter-Crazzolara, W. Keller, J. Biol. Chem. 266, 19768 (1991); A. Jenny, H.-P. Hauri, W. Keller. Mol. Cell. Biol. 14, 8183 (1994); A. Jenny and W. Keller, Nucleic Acids Res. 23, 2629 (1995).
13. S. Bienroth, E. Wahle, C. Suter-Crazzolara, W. Keller, J. Biol. Chem. 266, 19768 (1991); A. Jenny, H.-P. Hauri, W. Keller. Mol. Cell. Biol. 14, 8183 (1994); A. Jenny and W. Keller, Nucleic Acids Res. 23, 2629 (1995).
14. K. G. K, Murthy and J. L. Manley, J. Biol. Chem. 267, 14804 (1992); K. G. K. Murthy and J. L. Manley, Genes Dev. 9, 2672(1995).
15. K. G. K, Murthy and J. L. Manley, J. Biol. Chem. 267, 14804 (1992); K. G. K. Murthy and J. L. Manley, Genes Dev. 9, 2672(1995).
16. 2-terminal probe (24).
17. A. Jenny, L. Minvielle-Sebastia, P. J. Preker, W. Keller, unpublished data.
18. Tryptic peptides were obtained from the same preparative SDS-polyacrylamide gel as described (7).
19. A cDNA fragment starting at the Hind III site and containing the authentic stop codon was subcloned into pQE11 (Qiagen) and expressed in Escherichia coli (7). A rabbit was injected four times with 100 μg of protein (25). Monoclonal antibodies were obtained from the fusion described earlier (7).
20. C. J. Bult et al., Science 273, 1058 (1996); the M. jannaschii gene numbers are: MJ0047, MJ0162, and MJ1236.
21. M. Johnston, S. Andrews, R. Waterson, GenBank accession number U17245 (1994).
22. S. M. Noble and C. Gutnrie Genetics 143, 67 (1996).
23. G. Chanfreau, S. M. Noble, C. Guthrie, personal communication.
24. YSH1 was cloned by PCR and the screening of a genomic library (10). A truncated form of YSH1 starting at the internal Bgl II site and containing the authentic stop codon was subcloned into pQE10 (Qiagen) and expressed in E. coli (7). A rabbit was injected four times with 100 μg of SDS-polyacrylamide gel eluted fusion protein (25).
25. P. J. Preker, J. Lingner, L. Minvielle-Sebastia, W. Keller, Cell 81, 379 (1995).
26. P. J. Preker and W. Keller, in preparation.
27. E.-C. Park, D. Finley, J. W. Szostak, Proc. Natl. Acad. Sci. U.S.A. 89, 1249 (1992);
28. A. Varshavsky, Cold Spring Harbor Symp. Quant. Biol. 60, 461 (1996); plasmids were modified as follows: an Xho I-Bam HI cassette containing the CYC1 promoter, the ubiquitin coding sequence, and either a Met or Arg codon, was cloned between the GAL1 upstream-activating sequence, and a Not I cloning site (plasmids pGUM1 and pGUR1, respectively). These plasmids are centromeric and ADE2-marked (10). A Not I PCR (polymerase chain reaction) fragment carrying the complete open reading frame of YSH1 was introduced, yielding pGUM-YSH1 and pGUR-YSH1, respectively. Both plasmids can rescue a strain disrupted for the chromosomal copy of YSH1 on galactose medium. However, on 5% glucose medium, only the pGUM-YSH1-containing strain [LM112 (MATa, ysh1::TRP1; ura3-1; trp1 Δ; ade2-1; leu2-3,112; his3-11,15; and pGUM-YSH1)] is viable (LM111 is isogenic with LM112, except that it contains pGUR-YSH1).
29. Extracts were prepared as described [A. Ansari and B. Schwer, EMBO J. 14, 4001 (1995)]. The reactions were processed as described (5), except that in cleavage assays, cordycepine triphosphate (0.5 mM final concentration) replaced CTP, and magnesium acetate (1.8 mM) was used instead of EDTA.
30. J. Lingner, J. Kellermann, W. Keller, Nature 354, 496 (1991).
31. S. M. L. Barabino and W. Keller, unpublished data.
32. J. B. Olmstedt, J. Biol. Chem. 256, 11955 (1981); J. Sambrook, E. F. Fritsch, T. Maniatis, Molecular Cloning (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1989).
33. J. B. Olmstedt, J. Biol. Chem. 256, 11955 (1981); J. Sambrook, E. F. Fritsch, T. Maniatis, Molecular Cloning (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1989).
34. E. Harlow and D. Lane, Antibodies: A Laboratory Manual (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1988).
35. S. N. Cohen, Cell 80, 829 (1995).
36. We thank R. Pöhlmann for help in DNA sequencing, E.-C. Park and J. W. Szostak for plasmids, H. Pick and P. Philippsen for the yeast genomic library, G. Chanfreau, S. M. Noble, and C. Guthrie for communicating unpublished results, and U. Rüegsegger and E. Wahle for critically reading the manuscript. Supported by the Kantons of Basel, the Swiss National Science Foundation, a European Union long-term fellowship (Human Capital and Mobility Program. L.M.-S.), and a predoctoral fellowship from the Boehringer-Ingelheim Fonds (P.J.P.).