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Optimization and optimality of a short ribozyme ligase that joins non-Watson–Crick base pairings

Published online by Cambridge University Press:  09 April 2001

MICHAEL P. ROBERTSON ,
JAY R. HESSELBERTH  and
ANDREW D. ELLINGTON
MICHAEL P. ROBERTSON
Affiliation:
Department of Chemistry and Biochemistry, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA
JAY R. HESSELBERTH
Affiliation:
Department of Chemistry and Biochemistry, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA
ANDREW D. ELLINGTON
Affiliation:
Department of Chemistry and Biochemistry, Institute for Cellular and Molecular Biology, University of Texas at Austin, Austin, Texas 78712, USA
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Abstract

A small ribozyme ligase (L1) selected from a random sequence population appears to utilize non-Watson–Crick base pairs at its ligation junction. Mutational and selection analyses confirmed the presence of these base pairings. Randomization of the L1 core and selection of active ligases yielded highly active variants whose rates were on the order of 1 min−1. Base-pairing covariations confirmed the general secondary structure of the ligase, and the most active ligases contained a novel pentuple sequence covariation. The optimized L1 ligases may be optimal within their sequence spaces, and minimal ligases that span less than 60 nt in length have been engineered based on these results.

Keywords

ligaseribozyme
Type
Research Article
Information
RNA , Volume 7 , Issue 4 , April 2001 , pp. 513 - 523
Copyright
© 2001 RNA Society

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