The initiation codon AUG binds at a hydrophobic site on yeast 40S ribosomal subunits as revealed by fluorescence studies with bis (1,8-anilinonaphthalenesulfonate)

J. C. Lee, L. C.C. Yeh, P. M. Horowitz

Research output: Contribution to journalArticle

2 Scopus citations

Abstract

Binding studies of yeast 40S ribosome with bis (1,8-anilinonaphthalenesulfonate) (bis-ANS) revealed the binding of 3-4 molecules of bis-ANS per ribosome with a dissociation constant (Kd) of 1.45 μM. Binding of AUG to the 40S subunits resulted in a concentration-dependent decrease in the bis-ANS fluorescence without displacing all of the bound bis-ANS from the ribosomes. The residual bis-ANS fluorescence at saturation with AUG corresponds to about 3 molecules of bis-ANS per ribosome. Thus AUG displaces one of the bound bis-ANS molecules. The data suggest that AUG binds at a hydrophobic site on the yeast 40S subunit.

Original languageEnglish (US)
Pages (from-to)1245-1247
Number of pages3
JournalBiochimie
Volume73
Issue number9
DOIs
StatePublished - Sep 1991

Keywords

  • fluorescence
  • mRNA binding
  • protein hydrophobic surfaces
  • ribosome
  • yeast

ASJC Scopus subject areas

  • Biochemistry

Fingerprint Dive into the research topics of 'The initiation codon AUG binds at a hydrophobic site on yeast 40S ribosomal subunits as revealed by fluorescence studies with bis (1,8-anilinonaphthalenesulfonate)'. Together they form a unique fingerprint.

  • Cite this