Selective binding of amino add residues to tRNAPhe

Research output: Contribution to journalArticle

11 Citations (Scopus)

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
Externally publishedYes

Fingerprint

RNA, Transfer, Phe
Polynucleotides
Amides
Anticodon
Entropy
Phenylalanine
Tryptophan
Glycine
Amino acids
Quenching
Salts
Fluorescence
Amino Acids
Temperature
Protonation
Titration
Tyrosine
Conformations
Enthalpy
Conformation

ASJC Scopus subject areas

  • Statistics, Probability and Uncertainty
  • Applied Mathematics
  • Health, Toxicology and Mutagenesis
  • Toxicology
  • Genetics(clinical)
  • Genetics

Cite this

Selective binding of amino add residues to tRNAPhe . / Bujalowski, Wlodzimierz; Porschke, D.

In: Nucleic Acids Research, Vol. 12, No. 19, 11.10.1984, p. 7549-7563.

Research output: Contribution to journalArticle

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AB - 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.

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