Hammerhead redux: Does the new structure fit the old biochemical data?

  1. Jennifer A. Nelson and
  2. Olke C. Uhlenbeck
  1. Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, Evanston, Illinois 60208, USA

Abstract

The cleavage rates of 78 hammerhead ribozymes containing structurally conservative chemical modifications were collected from the literature and compared to the recently determined crystal structure of the Schistosoma mansoni hammerhead. With only a few exceptions, the biochemical data were consistent with the structure, indicating that the new structure closely resembles the transition state of the reaction. Since all the biochemical data were collected on minimal hammerheads that have a very different structure, the minimal hammerhead must be dynamic and occasionally adopt the quite different extended structure in order to cleave.

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Footnotes

  • Reprint requests to: Olke C. Uhlenbeck, Department of Biochemistry, Molecular Biology and Cell Biology, Northwestern University, 2205 Tech Drive, Hogan 2-100, Evanston, IL 60208, USA; e-mail: o-uhlenbeck{at}northwestern.edu; fax: (847) 491-5444.

  • Article published online ahead of print. Article and publication date are at http://www.rnajournal.org/cgi/doi/10.1261/rna.912608.

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