Ribosomal subunit antiassociation activity in rabbit reticulocyte lysates. Evidence for a low molecular weight ribosomal subunit antiassociation protein factor (M(r) = 25,000)

P. Raychaudhuri, E. A. Stringer, D. M. Valenzuela, U. Maitra

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Abstract

A ribosomal subunit antiassociation activity has been purified from both the postribosomal supernatant and ribosomal salt-wash protein fractions of rabbit reticulocyte lysates. A majority (> 90%) of the activity is associated with a low molecular weight protein of M(r) of approximately 25,000. A small but significant level of antiassociation activity (< 10%) was found to be associated with higher molecular weight protein fractions. The purified 25,000-dalton antiassociation factor interacts with 60 S ribosomal subunits to prevent them from reassociating with 40 S ribosomal subunits. The factor does not seem to interact directly with 40 S subunits nor does it dissociate 80 S monosomes. The properties of this factor are thus similar to the eukaryotic initiation factor 6 isolated from both wheat germ and calf liver extracts.

Original languageEnglish (US)
Pages (from-to)11930-11935
Number of pages6
JournalJournal of Biological Chemistry
Volume259
Issue number19
StatePublished - Jan 1 1984

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ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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