Abstract
The assembly of the spliceosome is an ATP-dependent process. The splicing factor PRP16 contains variations of several motifs that define the elF-4A-like ATP-dependent RNA helicase family. The protein has now been purified and shown to exhibit RNA-dependent ATPase activity. PRP16 is required specifically for the second catalytic step of the splicing reaction in vitro. This function requires ATP binding and/or hydrolysis, which appears to be concomitant with release of the protein from the spliceosome. PRP16 may be the prototype for a set of splicing factors which use ATP to drive a cycle of conformational changes.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Cech, T. R. & Bass, B. L. A. Rev. Biochem. 55, 599–629 (1986).
Sharp, P. A. Science 235, 766–771 (1987).
Guthrie, C. Am. Zool. 29, 557–567 (1989).
Michel, F., Umesono, K. & Ozeki, H. Gene 82, 5–30 (1989).
Green, M. R. A. Rev. Genet. 20, 671–708 (1986).
Woolford, J. L. Jr Yeast 5, 435–457 (1989).
Guthrie, C. & Patterson, B. A. Rev. Genet 23, 387–419 (1988).
Lührmann, R. in Structure and Function of Major and Minor Small Nuclear Ribonucleoprotein Particles (ed. Birnstiel, M. L.), 71–99 (Springer, Berlin, 1988).
Cheng, S. C. & Abelson, J. Genes Dev. 1, 1014–1027 (1987).
Konarska, M. M. & Sharp, P. A. Cell 49, 763–774 (1987).
Hartwell, L. H. J. Bact. 93, 1662–1670 (1967).
Vijayraghavan, U., Company, M. & Abelson, J. Genes Dev. 3, 1206–1216 (1989).
Lustig, A. J., Lin, R. J. & Abelson, J. Cell 47, 953–963 (1986).
Vijayraghavan, U. & Abelson, J. Molec cell. Biol. 10, 324–332 (1990).
Lossky, M., Anderson, G. J., Jackson, S. P. & Beggs, J. Cell 51, 1019–1026 (1987).
Banroques, J. & Abelson, J. Molec cell. Biol. 9, 3710–3719 (1989).
Bjørn, S. P., Soltyk, A., Beggs, J. D. & Friesen, J. D. Mol. cell. Biol. 9, 3698–3709 (1989).
Chang, T. H., Clark, M. W., Lustig, A. J., Cusick, M. E. & Abelson, J. Molec. cell. Biol. 8, 2379–2393 (1988).
Whittaker, E., Lossky, M. & Beggs, J. D. Proc. natn. Acad. Sci. U.S.A. 87, 2216–2219 (1990).
Lin, R. J., Lustig, A. J. & Abelson, J. Genes Dev. 1, 7–18 (1987).
Couto, J. R., Tamm, J., Parker, R. & Guthrie, C. Genes Dev. 1, 445–455 (1987).
Burgess, S., Couto, J. R. & Guthrie, C. Cell. 60, 705–717 (1990).
Rozen, F. et al. Molec. cell. Biol. 10, 1134–1144 (1990).
Linder, P. et al. Nature 337, 121–122 (1989).
Schena, M., Picard, D. & Yamamoto, K. R. Meth. Enzym. 194, 389–398 (1990).
Lin, R. J., Newman, A. J., Cheng, S. C. & Abelson, J. J. biol. Chem. 260, 14780–14792 (1985).
England, T. E. & Uhlenbeck, O. C. Nature 275, 560–561 (1978).
Cheng, S. C. & Abelson, J. Proc. natn. Acad. Sci. U.S.A. 83, 2387–2391 (1986).
MacArthur, H. & Walter, G. J. Virol. 52, 483–491 (1984).
Clark, R., Lane, D. P. & Tjian, R. J. biol. Chem. 256, 11854–11858 (1981).
Grifo, J. A., Abramson, R. D., Satler, C. A. & Merrick, W. C. J. biol. Chem. 259, 8648–8654 (1984).
Nishi, K., Morel-Deville, F., Hershey, J. W. B., Leighton, T. & Schnier, J. Nature 336, 496–498 (1988).
Hirling, H., Scheffner, M., Restle, T. & Stahl, H. Nature 339, 562–564 (1989).
Iggo, R. D. & Lane, D. P. EMBO J. 8, 1827–1831 (1989).
Sawa, H., Ohno, M., Sakamoto, H. & Shimura, Y. Nucleic Acids Res. 16, 3157–3164 (1988).
Sergeant, A., Bohmann, D., Zentgraf, H., Weiher, H. & Keller, W. J. molec. Biol. 180, 577–600 (1984).
Thompson, R. C. Trends biochem. Sci. 13, 91–93 (1988).
Chang, T. H., Arenas, J. & Abelson, J. Proc. natn. Acad. Sci. U.S.A. 87, 1571–1575 (1990).
Dalbadie-McFarland, G. & Abelson, J. Proc. natn. Acad. Sci. U.S.A. 87, 4236–4240 (1990).
Hodgman, T. C. Nature 333, 22–23 (1988).
Rhoads, R. E. Trends biochem. Sci. 13, 52–56 (1988).
Gualerzi, C. O. & Pon, C. L. Biochemistry 29, 5881–5889 (1990).
Towbin, H., Staehelin, T. & Gordon, J. Proc. natn. Acad. Sci. U.S.A. 76, 4350–4354 (1979).
Spindler, K. R., Rosser, D. S. E. & Berk, A. J. J. Virol. 49, 132–141 (1984).
Snyder, M. J. Cell Biol. 108, 1419–1429 (1989).
Ito, H., Fukuda, Y., Murata, K. & Kimura, A. J. Bact. 153, 163–168 (1983).
Wray, W., Boulikas, T., Wray, V. P. & Hancock, R. Analyt. Biochem. 118, 197–203 (1981).
Bradford, M. M. Analyt Biochem. 72, 248–254 (1976).
Barnes, D. A. & Thorner, J. Molec. cell. Biol. 6, 2828–2838 (1986).
Hamm, J. Kazmaier, M. & Mattaj, I. W. EMBO J. 6, 3479–3485 (1987).
Company, M., Arenas, J. & Abelson, J. Nature 349, 487–493 (1991).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Schwer, B., Guthrie, C. PRP16 is an RNA-dependent ATPase that interacts transiently with the spliceosome. Nature 349, 494–499 (1991). https://doi.org/10.1038/349494a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/349494a0
This article is cited by
-
Structure of a spliceosome remodelled for exon ligation
Nature (2017)
-
Cryo-EM structure of a human spliceosome activated for step 2 of splicing
Nature (2017)
-
Mechanistic insights into precursor messenger RNA splicing by the spliceosome
Nature Reviews Molecular Cell Biology (2017)
-
Functional roles of DExD/H-box RNA helicases in Pre-mRNA splicing
Journal of Biomedical Science (2015)
-
Evidence for a group II intron–like catalytic triplex in the spliceosome
Nature Structural & Molecular Biology (2014)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.