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Science 5 June 1992:
Vol. 256. no. 5062, pp. 1420 - 1424
DOI: 10.1126/science.1604316
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Articles
Science, Vol 256, Issue 5062, 1420-1424
Copyright © 1992 by American Association for the Advancement of Science
Aminoacyl esterase activity of the Tetrahymena ribozyme
JA Piccirilli,
TS McConnell,
AJ Zaug,
HF Noller,
and
TR Cech
Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.
Several classes of ribozymes (catalytic RNA's) catalyze reactions at phosphorus centers, but apparently no reaction at a carbon center has been demonstrated. The active site of the Tetrahymena ribozyme was engineered to bind an oligonucleotide derived from the 3' end of N-formyl-methionyl-tRNA(fMet). This ribozyme catalyzes the hydrolysis of the aminoacyl ester bond to a modest extent, 5 to 15 times greater than the uncatalyzed rate. Catalysis involves binding of the oligonucleotide to the internal guide sequence of the ribozyme and requires Mg2+ and sequence elements of the catalytic core. The ability of RNA to catalyze reactions with aminoacyl esters expands the catalytic versatility of RNA and suggests that the first aminoacyl tRNA synthetase could have been an RNA molecule.
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