Nucleic Acids Research, 1994, Vol. 22, No. 23 5031-5037
© 1994
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Histidylation by yeast HisRS of tRNA or tRNA-like structure relies on residues–1 and 73 but is dependent on the RNA context
Unité propre de Recherche 9002 ‘Structure des Macromolécules Biologiques et Mécanismes de Reconnaissance’, Institut de Biologie Moléculaire et Cellulaire du Centre National de la Recharche Scientifique 15 rue René Descartes, F–67084 Strasbourg Cedex, France
*To whom correpsondence should be addressed
Received August 5, 1994. Revised October 26, 1994. Accepted October 26, 1994.
Residue G–1 and discriminator base C73 are the major histidine identity elements in prokaryotes. Here we evaluate the importance of these two nucleotides in yeast histidine aminoacylation identity. Deletion of G–1 in yeast tRNAHis transcript leads to a drastic loss of histidylation specificity (about 500-fold). Mutation of discriminator base A73, common to all yeast tRNAHis species, into G73 has a more moderate but still significant effect with a 22-fold decrease in histidylation specificity. Changes at position 36 in the anticodon loop has negligible effect on histidylation. The role of residues –1 and 73 for specific aminoacylation by yeast HisRS was further investigated by studying the histidylation capacities of seven minihelices derived from the Turnip Yellow Mosaic Virus tRNA-like structure. Changes in the nature of nucleotides –1 and 73 modulate this activity but do not suppress it. The optimal mini-substrate for HisRS presents a G-A mismatch at the position equivalent to residues G–1 A73 in yeast tRNAHis, confirms the importance of this structural feature in yeast histidine identity. The fact that the minisubstrates contain a pseudoknot in which position -1 is mimicked by an internal nucleo-tide from the pseudoknot highlights further the necessity of a stacking interaction of this position over the amino acid accepting branch of the tRNA during the aminoacylation process. Individual transplantation of G.t or A73 into yeast tRNAAsp transcript improves the histidylation efficiency of the engineered tRNAAsp. However, a tRNAAsp transcript presenting simultan-eously both residues G–1 and A73 becomes a less good substrate for HisRS, suggesting the importance of the structural context and/or the presence of anti-determinants for an optimal expression of these two identity elements.
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