Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Site Tools

  • AAAS
  • Subscribe
  • Feedback

Site Search

Search Advanced

Science 22 September 2006:
Vol. 313. no. 5794, pp. 1752 - 1756
DOI: 10.1126/science.1129666
Prev | Table of Contents | Next

Research Articles

Structural Basis of glmS Ribozyme Activation by Glucosamine-6-Phosphate

Daniel J. Klein and Adrian R. Ferré-D'Amaré*

The glmS ribozyme is the only natural catalytic RNA known to require a small-molecule activator for catalysis. This catalytic RNA functions as a riboswitch, with activator-dependent RNA cleavage regulating glmS messenger RNA expression. We report crystal structures of the glmS ribozyme in precleavage states that are unliganded or bound to the competitive inhibitor glucose-6-phosphate and in the postcleavage state. All structures superimpose closely, revealing a remarkably rigid RNA that contains a preformed active and coenzyme-binding site. Unlike other riboswitches, the glmS ribozyme binds its activator in an open, solvent-accessible pocket. Our structures suggest that the amine group of the glmS ribozyme-bound coenzyme performs general acid-base and electrostatic catalysis.

Division of Basic Sciences, Fred Hutchinson Cancer Research Center, 1100 Fairview Avenue North, Seattle, WA 98109–1024, USA.

* To whom correspondence should be addressed. E-mail: aferre{at}fhcrc.org

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Riboswitch effectors as protein enzyme cofactors.
J. C. Cochrane and S. A. Strobel (2008)
RNA 14, 993-1002
   Abstract »    Full Text »    PDF »
Complex Riboswitches.
R. R. Breaker (2008)
Science 319, 1795-1797
   Abstract »    Full Text »    PDF »
Mechanism of mRNA destabilization by the glmS ribozyme.
J. A. Collins, I. Irnov, S. Baker, and W. C. Winkler (2007)
Genes & Dev. 21, 3356-3368
   Abstract »    Full Text »    PDF »
Riboswitch Control of Gene Expression in Plants by Splicing and Alternative 3' End Processing of mRNAs.
A. Wachter, M. Tunc-Ozdemir, B. C. Grove, P. J. Green, D. K. Shintani, and R. R. Breaker (2007)
PLANT CELL 19, 3437-3450
   Abstract »    Full Text »    PDF »
Guanine riboswitch variants from Mesoplasma florum selectively recognize 2'-deoxyguanosine.
J. N. Kim, A. Roth, and R. R. Breaker (2007)
PNAS 104, 16092-16097
   Abstract »    Full Text »    PDF »
Metal-ion binding and metal-ion induced folding of the adenine-sensing riboswitch aptamer domain.
J. Noeske, H. Schwalbe, and J. Wohnert (2007)
Nucleic Acids Res.
   Abstract »    Full Text »    PDF »
Improved native affinity purification of RNA.
R. T. Batey and J. S. Kieft (2007)
RNA 13, 1384-1389
   Abstract »    Full Text »    PDF »
A comparison of vanadate to a 2'-5' linkage at the active site of a small ribozyme suggests a role for water in transition-state stabilization.
A. T. Torelli, J. Krucinska, and J. E. Wedekind (2007)
RNA 13, 1052-1070
   Abstract »    Full Text »    PDF »
Trans-acting glmS catalytic riboswitch: Locked and loaded.
R. A. Tinsley, J. R.W. Furchak, and N. G. Walter (2007)
RNA 13, 468-477
   Abstract »    Full Text »    PDF »
Core requirements of the adenine riboswitch aptamer for ligand binding.
J.-F. Lemay and D. A. Lafontaine (2007)
RNA 13, 339-350
   Abstract »    Full Text »    PDF »


ADVERTISEMENT
Click Me!

ADVERTISEMENT
Click Me!

To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)