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Nucleic Acids Research, 1995, Vol. 23, No. 22 4598-4602
© 1995

Articles

Footprinting of tRNAPhe transcripts from Thermus thermophilus HB8 with the homologues phenylalanyl-tRNA synthetase reveals a novel mode of interaction

Roland Kreutzer*, Daniel Kern, R. Giegè1 and Joëlle Rudinger

Lehrstuhl für Biochemie, Universität Bayreuth, UniversitätsstraBe 30 95440 Bayreuth, Germany 1UPR9002 Structure des Macromolecules Biologiques de Reconnaissance, Institut de Biologie Moleculaire et Cellulaire du Centre National de la Recherche Scientifiqu 15 rue Rene Descartes, 67084 Strasbourg, France

*To whom correspondence should be addressed

Received September 1, 1995. Accepted October 12, 1995.

The phosphates of the tRNAPhe transcript from Thermus thermophilus interacting with the cognate synthetase were determined by footprinting. Backbone bond protection against cleavage by iodine of the phosphorothioate- containing transcripts was found in the arrdcodon stem-loop, the D stem-loop and the acceptor stem and weak protection was also seen in the variable loop. Most of the protected phosphates correspond to regions around known identity elements of tRNAPhe. Enhancement of cleavage at certain positions indicates bending of tRNAPhe upon binding to the enzyme. When applied to the three-dimensional model of tRNAPhe from yeast the majority of the protections occur on the D loop side of the molecule, revealing that phenylalanyl-tRNA synthetase has a rather complex and novel pattern of interaction with tRNAPhe, differing from that of other known class II aminoacyl-tRNA synthetases.


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