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Structural studies on tRNA acceptor stem microhelices : exchange of the discriminator base A73 for G in human tRNAᴸᵉᵘ switches the acceptor specificity from leucine to serine possibly by decreasing the stability of the terminal G1-C72 base pair

Title data

Metzger, Armin U. ; Heckl, Martha ; Willbold, Dieter ; Breitschopf, Kristin ; RhajBandhary, Uttam L. ; Rösch, Paul ; Gross, Hans Joachim:
Structural studies on tRNA acceptor stem microhelices : exchange of the discriminator base A73 for G in human tRNAᴸᵉᵘ switches the acceptor specificity from leucine to serine possibly by decreasing the stability of the terminal G1-C72 base pair.
In: Nucleic Acids Research. Vol. 25 (November 1997) Issue 22 . - pp. 4551-4556.
ISSN 1362-4962
DOI: https://doi.org/10.1093/nar/25.22.4551

Abstract in another language

Correct recognition of transfer RNAs (tRNAs) by aminoacyl-tRNA synthetases (aaRS) is crucial to the maintenance of translational fidelity. The discriminator base A73 in human tRNALeuis critical for its specific recognition by the aaRS. Exchanging A73 for G abolishes leucine acceptance and converts it into a serine acceptor in vitro . Two RNA microhelices of 24 nt length that correspond to the tRNALeuacceptor stem and differ only in the discriminator base were synthesized: a wild-type tRNALeumicrohelix, where nt 21 corresponds to the discriminator base position 73, and an A21G mutant microhelix. To investigate whether different identities of both tRNAs are caused by conformational differences, NMR and UV melting experiments were performed on both microhelices. Two-dimentional NOESY spectra showed both microhelices to exhibit the same overall conformation at their 3'-CCA ends. Thermodynamic analysis and melting behaviour of the base-paired imino protons observed by NMR spectroscopy suggest that the A21G (A73G in tRNA) exchange results in a decrease of melting transition cooperativity and a destabilization of the terminal G1-C20 (G1-C72 in tRNA) base pair. Furthermore, the fact that this 3'-terminal imino proton is more solvent-exposed at physiological temperature might be another indication for the importance of the stability of the terminal base pair for specific tRNA recognition.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors > Chair Biopolymers - Univ.-Prof. Dr. Paul Rösch
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Former Professors
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biopolymers
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 540 Chemistry
500 Science > 570 Life sciences, biology
Date Deposited: 15 Jan 2019 13:31
Last Modified: 16 May 2019 05:37
URI: https://eref.uni-bayreuth.de/id/eprint/46904