Removal of Y-37 from tRNAyeastphe alters oligomer binding to two loops

Vicki Cameron*, Olke C. Uhlenbeck

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

21 Scopus citations

Abstract

The association constants of complementary oligomers were used to monitor changes in the structure of tRNAyeastphe as a consequence of excision of a single base Y in the anticodon loop and of clipping the molecule at the point of excision. Significant changes were found not only in the binding constants of oligomers complementary to the anticodon loop but also in the K of an oligomer complementary to the dihydro U loop. The results suggest that either a single base change in a tRNA may alter structure elsewhere in the molecule or that the acid treatment necessary to remove Y irreversibly alters the structure of tRNAyeastphe.

Original languageEnglish (US)
Pages (from-to)635-640
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume50
Issue number3
DOIs
StatePublished - Feb 5 1973

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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