Wheat germ initiation factors 4F and (iso)4F interact differently with oligoribonucleotide analogues of rabbit alpha-globin mRNA

Biochemistry. 1991 May 7;30(18):4542-5. doi: 10.1021/bi00232a025.

Abstract

The binding of capped oligoribonucleotide analogues of the 5' terminus of rabbit alpha-globin mRNA to wheat germ protein synthesis initiation factors eIF-4F and eIF-(iso)4F was measured by direct fluorescence techniques. An analysis of the equilibrium association constants (Keq) indicates that both eIF-4F and eIF-(iso)4F recognize primarily the m7G cap structure but differ in the recognition of other structural features. eIF-4F is sensitive to the position and sequence of hairpin structures within the oligoribonucleotide, while eIF-(iso)4F shows a preference for linear sequences. These differences suggest that wheat germ eIF-4F and eIF-(iso)4F may have discriminatory activity for mRNA recognition.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Base Sequence
  • Eukaryotic Initiation Factor-4F
  • Eukaryotic Initiation Factors*
  • Fluorescence
  • Globins / genetics*
  • Molecular Sequence Data
  • Nucleic Acid Conformation
  • Oligonucleotides / genetics
  • Peptide Initiation Factors / genetics*
  • RNA Caps / chemistry
  • RNA, Messenger / metabolism*
  • Rabbits
  • Seeds / genetics
  • Triticum / genetics*

Substances

  • Eukaryotic Initiation Factor-4F
  • Eukaryotic Initiation Factors
  • Oligonucleotides
  • Peptide Initiation Factors
  • RNA Caps
  • RNA, Messenger
  • eIF-4B
  • Globins