Determination of the angle between the anticodon and aminoacyl acceptor stems of yeast phenylalanyl tRNA in solution

Marisa W. Friederich, Frank Ulrich Gast, Elsi Vacano, Paul J Hagerman

Research output: Contribution to journalArticle

35 Scopus citations

Abstract

A principal feature of the crystal structures of tRNAs is an L-shaped tertiary conformation in which the aminoacyl acceptor stem and the anticodon stem are approximately perpendicular. However, the anticodon-acceptor interstem angle has not been precisely quantified in solution for any tRNA. Such a determination would represent an important test of the predicted global conformation of tRNAs in solution. To this end, we have constructed a yeast tRNA(Phe) heteroduplex RNA molecule in which the anticodon and acceptor stems of the tRNA have each been extended by approximately 70 base pairs. A comparison of the rotational decay times of the heteroduplex molecule and a linear control yields an interstem angle of 89 ± 4° in 4 mM magnesium chloride/100 μM spermine hydrochloride, essentially identical to the corresponding angle observed in the crystal under similar buffer and temperature conditions. The current approach is applicable to the study of a wide variety of RNA molecules that possess elements of nonhelical structure.

Original languageEnglish (US)
Pages (from-to)4803-4807
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number11
DOIs
StatePublished - May 23 1995
Externally publishedYes

Keywords

  • gel electrophoresis
  • protein biosynthesis
  • RNA structure
  • transcription
  • transient electric birefringence

ASJC Scopus subject areas

  • Genetics
  • General

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