Nucleic Acids Research, Vol 25, Issue 24 4899-4906, Copyright © 1997 by Oxford University Press
M Sissler, G Eriani, F Martin, R Giege and C Florentz
Gene cloning, overproduction and an efficient purification protocol of
yeast arginyl-tRNA synthetase (ArgRS) as well as the interaction patterns
of this protein with cognate tRNAArgand non-cognate tRNAAspare described.
This work was motivated by the fact that the in vitro transcript of
tRNAAspis of dual aminoacylation specificity and is not only aspartylated
but also efficiently arginylated. The crystal structure of the complex
between class II aspartyl-tRNA synthetase (AspRS) and tRNAAsp, as well as
early biochemical data, have shown that tRNAAspis recognized by its
variable region side. Here we show by footprinting with enzymatic and
chemical probes that transcribed tRNAAspis contacted by class I ArgRS along
the opposite D arm side, as is homologous tRNAArg, but with idiosyncratic
interaction patterns. Besides protection, footprints also show enhanced
accessibility of the tRNAs to the structural probes, indicative of
conformational changes in the complexed tRNAs. These different patterns are
interpreted in relation to the alternative arginine identity sets found in
the anticodon loops of tRNAArgand tRNAAsp. The mirror image alternative
interaction patterns of unmodified tRNAAspwith either class I ArgRS or
class II AspRS, accounting for the dual identity of this tRNA, are
discussed in relation to the class defining features of the synthetases.
This study indicates that complex formation between unmodified tRNAAspand
either ArgRS and AspRS is solely governed by the proteins.
ARTICLES
Mirror image alternative interaction patterns of the same tRNA with either class I arginyl-tRNA synthetase or class II aspartyl-tRNA synthetase
Unite Propre de Recherche 9002 'Structure des Macromolecules Biologiques et Mecanismes de Reconnaissance', Institut de Biologie Moleculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France.
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