Selective binding of amino add residues to tRNAPhe

W. Bujalowski, D. Porschke

    Research output: Contribution to journalArticlepeer-review

    11 Scopus citations

    Abstract

    The interaction of amino acid amides with tRNAPhe was studied by measurements of the Wye base fluorescence. Binding of phenylalanine-, tyrosine- and tryptophan-amides leads to considerable quenching, whereas the asides of e.g. glycine and lencine do not induce quenching nnder the sane conditions. Binding constants at 0,13 M salt - 100 M-1 for Phe-, 110 M-1 for Tyr- and 300 M-1 for Trp-amide - are about a factor of 6 higher than those evaluated from independent measurements for binding to simple single-stranded polynucleotides; the corresponding factor is 10 for double-stranded polynucleotides. Since the apparent enthalpy changes derived from measurements at different temperatures remains relatively low (-9 to -20 kJ/mol), the increased affinity appears to be mainly due to an increase of the entropy changes. Titration experiments performed in the presence of Mg2+ indicate cooperative interactions of the aromatio residues with the anticodon loop that are consistent with preferential binding to one of two loop conformations. Measurements of binding constants at different pH-values indicate the protonation of a tENA residue in the tryptophanamido-tRNAPhe oomplex characterised by a pK value of about 7.0.

    Original languageEnglish (US)
    Pages (from-to)7549-7563
    Number of pages15
    JournalNucleic acids research
    Volume12
    Issue number19
    DOIs
    StatePublished - Oct 11 1984

    ASJC Scopus subject areas

    • Genetics

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