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Nucleic Acids Research, 1993, Vol. 21, No. 1 41-49
© 1993

MOLECULAR BIOLOGY

Influence of tRNA tertiary structure and stability on aminoacylation by yeast aspartyl-tRNA synthetase

Joseph D. Puglisi+, Joern Pütz, Catherine Florentz and Richard Giegé*

UPR Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance, Institut de Biologie Moléculaire et Cellulaire du CNRS 15 rue René Descartes, F-67084 Strasbourg Cedex, France

*To whom correspondence should be addressed

Received October 26, 1992. Accepted December 4, 1992.

Mutations have been designed that disrupt the tertiary structure of yeast tRNAAsp. The effects of these mutations on both tRNA structure and specific aspartylatlon by yeast aspartyl-tRNA synthetase were assayed. Mutations that disrupt tertiary Interactions Involving the D-stem or D-loop result In destablllzatlon of the base-pairing In the D-stem, as monitored by nuclease digestion and chemical modification studies. These mutations also decrease the specificity constant (KcatKm) for aspartylatlon by aspartyl-tRNA synthetase up to 103–104 fold. The size of the T-loop also influences tRNAAsp structure and function; change of Its T-loop to a tetraloop (-UUCG-) sequence results in a denatured D-stem and an almost 104 fold decrease of kcatKmfor aspartylation. The negative effects of these mutations on aspartylation activity are significantly alleviated by additional mutations that stabilize the D-stem. These results indicate that a critical role of tertiary structure In tRNAAsp for aspartylation is the maintenance of a base-paired D-stem.

+Present address: Department of Chemistry, Massachusetts Institute of Technology, 77 Massachusetts Avenue, Cambridge MA 02139, USA


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