Joining the two domains of a group I ribozyme to form the catalytic core

Science

Volumn 275, Issue 5301, 1997, Pages 847-849

  Tanner, Michael A ^a   Cech, Thomas R ^a  

^a UNIVERSITY OF COLORADO   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

RIBOZYME;

ARTICLE; BINDING SITE; CATALYSIS; ENZYME ACTIVE SITE; KINETICS; PRIORITY JOURNAL; RNA SPLICING;

ANABAENA; ANIMALS; BASE COMPOSITION; BINDING SITES; GUANOSINE; INTRONS; MUTAGENESIS, SITE-DIRECTED; NUCLEIC ACID CONFORMATION; RNA SPLICING; RNA, BACTERIAL; RNA, CATALYTIC; RNA, PROTOZOAN; TETRAHYMENA;

EID: 0031025796     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.275.5301.847     Document Type: Article

References (44)

1. T. R. Cech, Annu. Rev. Biochem. 59, 543 (1990).
2. F. Michel and E. Westhof, J. Mol. Biol. 216, 585 (1990).
3. F. L. Murphy and T. R. Cech, Biochemistry 32, 5291 (1993); J. Mol. Biol. 236, 49 (1994).
4. F. L. Murphy and T. R. Cech, Biochemistry 32, 5291 (1993); J. Mol. Biol. 236, 49 (1994).
5. J.-F. Wang, W. D. Downs, T. R. Cech, Science 260, 504 (1993).
6. F. Michel et al., Nature 342, 391 (1989).
7. J. A. Doudna and T. R. Cech, RNA 1, 36 (1995).
8. D. Gautheret, S. H. Damberger, R. R. Gutell, J. Mol. Biol. 248, 27 (1995).
9. R. R. Gutell, unpublished data.
10. B. Reinhold-Hurek and D. A. Shub, Nature 357, 173 (1992).
11. M. A. Tanner and T. R. Cech, RNA 2, 74 (1996).
12. M.-Q. Xu et al., Science 250, 1566 (1990); A. J. Zaug, J. A. Dávila-Aponte, T. R. Cech, Biochemistry 33, 14935 (1994); B. L. Golden and T. R. Cech, ibid. 35, 3754 (1996).
13. M.-Q. Xu et al., Science 250, 1566 (1990); A. J. Zaug, J. A. Dávila-Aponte, T. R. Cech, Biochemistry 33, 14935 (1994); B. L. Golden and T. R. Cech, ibid. 35, 3754 (1996).
14. M.-Q. Xu et al., Science 250, 1566 (1990); A. J. Zaug, J. A. Dávila-Aponte, T. R. Cech, Biochemistry 33, 14935 (1994); B. L. Golden and T. R. Cech, ibid. 35, 3754 (1996).
15. A. J. Zaug, M. M. McEvoy, T. R. Cech, Biochemistry 32, 7946 (1993).
16. 32P]ATP, and the RNA was gel-purified as described (10).
17. M. A. Tanner and T. R. Cech, unpublished data.
18. The Tetrahymena intron mutants were constructed by PCR as before and cloned into the pBGST7 vector (16) at the unique restriction sites Sph I (in P2) and Nhe I (in P9). Preparation of precursor RNA was the same as for Anabaena (13).
19. J. V. Price and T. R. Cech, Science 228, 719 (1985); M. D. Been and T. R. Cech, Cell 47, 207 (1986).
20. J. V. Price and T. R. Cech, Science 228, 719 (1985); M. D. Been and T. R. Cech, Cell 47, 207 (1986).
21. A. J. Zaug, P. J. Grabowski, T. R. Cech, Nature 301, 578 (1983); K. Ehrenman et al., Proc. Natl. Acad. Sci. U.S.A. 83, 5875 (1986); H. F. Tabak et al., Cell 48, 101 (1987).
22. A. J. Zaug, P. J. Grabowski, T. R. Cech, Nature 301, 578 (1983); K. Ehrenman et al., Proc. Natl. Acad. Sci. U.S.A. 83, 5875 (1986); H. F. Tabak et al., Cell 48, 101 (1987).
23. A. J. Zaug, P. J. Grabowski, T. R. Cech, Nature 301, 578 (1983); K. Ehrenman et al., Proc. Natl. Acad. Sci. U.S.A. 83, 5875 (1986); H. F. Tabak et al., Cell 48, 101 (1987).
24. The Tetrahymena intron contains extra sequence elements in P2.1, the P5abc extension, and the P9 extension, some of which stabilize the core (3, 19). The Anabaena intron lacks these extra elements and presumably relies more on core interactions forfolding of the active site.
25. G. F. Joyce, G. van der Horst, T. Inoue, Nucleic Acids Res. 17, 7879 (1989); B. Laggerbauer, F. L. Murphy, T. R. Cech, EMBO J. 13, 2669 (1994); P. P. Zarrinkar and J. R. Williamson, Nucleic Acids Res. 24, 854 (1996).
26. G. F. Joyce, G. van der Horst, T. Inoue, Nucleic Acids Res. 17, 7879 (1989); B. Laggerbauer, F. L. Murphy, T. R. Cech, EMBO J. 13, 2669 (1994); P. P. Zarrinkar and J. R. Williamson, Nucleic Acids Res. 24, 854 (1996).
27. G. F. Joyce, G. van der Horst, T. Inoue, Nucleic Acids Res. 17, 7879 (1989); B. Laggerbauer, F. L. Murphy, T. R. Cech, EMBO J. 13, 2669 (1994); P. P. Zarrinkar and J. R. Williamson, Nucleic Acids Res. 24, 854 (1996).
28. Context effects on base triples have been observed in tRNA by comparative analysis [R. R. Gutell et al., Nucleic Acids Res. 20, 5785 (1992)] and experimentally in the triple helix scaffold of group I introns (24, 25).
29. J. H. Cate et al., Science 273, 1678 (1996).
30. S. Lacks, Genetics 53, 207 (1966); V. B. Zhurkin et al., J. Mol. Biol. 239, 181 (1994).
31. S. Lacks, Genetics 53, 207 (1966); V. B. Zhurkin et al., J. Mol. Biol. 239, 181 (1994).
32. S. C. Schultz, G. C. Shields, T. A. Steitz, Science 253, 1001 (1991); L. V. Meervelt et al., Nature 374, 742 (1995); D. Vlieghe et al., Science 273, 1702 (1996).
33. S. C. Schultz, G. C. Shields, T. A. Steitz, Science 253, 1001 (1991); L. V. Meervelt et al., Nature 374, 742 (1995); D. Vlieghe et al., Science 273, 1702 (1996).
34. S. C. Schultz, G. C. Shields, T. A. Steitz, Science 253, 1001 (1991); L. V. Meervelt et al., Nature 374, 742 (1995); D. Vlieghe et al., Science 273, 1702 (1996).
35. F. Michel et al., Nature 347, 578 (1990).
36. R. Green and J. W. Szostak, J. Mol. Biol. 235, 140 (1994).
37. M. E. Harris et al., EMBO J. 13, 3953 (1994); A. M. Pyle and J. B. Green, Biochemistry 33, 2716 (1994); M. Costa and F. Michel, EMBO J. 14, 1276 (1995); T. Pan, Biochemistry 34, 902 (1995); for ribosomal RNA, see R. R. Gutell, in Ribosomal RNA, R. A. Zimmermann and A. E. Dahlberg, Eds. (CRC Press, Boca Raton, FL, 1996), pp. 111-128, and references therein.
38. M. E. Harris et al., EMBO J. 13, 3953 (1994); A. M. Pyle and J. B. Green, Biochemistry 33, 2716 (1994); M. Costa and F. Michel, EMBO J. 14, 1276 (1995); T. Pan, Biochemistry 34, 902 (1995); for ribosomal RNA, see R. R. Gutell, in Ribosomal RNA, R. A. Zimmermann and A. E. Dahlberg, Eds. (CRC Press, Boca Raton, FL, 1996), pp. 111-128, and references therein.
39. M. E. Harris et al., EMBO J. 13, 3953 (1994); A. M. Pyle and J. B. Green, Biochemistry 33, 2716 (1994); M. Costa and F. Michel, EMBO J. 14, 1276 (1995); T. Pan, Biochemistry 34, 902 (1995); for ribosomal RNA, see R. R. Gutell, in Ribosomal RNA, R. A. Zimmermann and A. E. Dahlberg, Eds. (CRC Press, Boca Raton, FL, 1996), pp. 111-128, and references therein.
40. M. E. Harris et al., EMBO J. 13, 3953 (1994); A. M. Pyle and J. B. Green, Biochemistry 33, 2716 (1994); M. Costa and F. Michel, EMBO J. 14, 1276 (1995); T. Pan, Biochemistry 34, 902 (1995); for ribosomal RNA, see R. R. Gutell, in Ribosomal RNA, R. A. Zimmermann and A. E. Dahlberg, Eds. (CRC Press, Boca Raton, FL, 1996), pp. 111-128, and references therein.
41. M. E. Harris et al., EMBO J. 13, 3953 (1994); A. M. Pyle and J. B. Green, Biochemistry 33, 2716 (1994); M. Costa and F. Michel, EMBO J. 14, 1276 (1995); T. Pan, Biochemistry 34, 902 (1995); for ribosomal RNA, see R. R. Gutell, in Ribosomal RNA, R. A. Zimmermann and A. E. Dahlberg, Eds. (CRC Press, Boca Raton, FL, 1996), pp. 111-128, and references therein.
42. T. R. Cech, S. H. Damberger, R. R. Gutell, Nature Struct. Biol. 1, 273 (1994).
43. J.-F. Wang and T. R. Cech, Science 256, 526 (1992).
44. Supported by NIH grant GM28039, and the Howard Hughes Medical Institute (T.C.R.). We thank the W. M. Keck Foundation for support of RNA Science on the Boulder campus; R. Gutell for assisting us with sequence analysis; R. Gutell and B. Golden for comments on the manuscript; and C. Grosshans and E. Podell for synthesizing oligodeoxynucleotides.