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 - 1984

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Ribosome Subunits
Reticulocytes
Molecular Weight
Molecular weight
Rabbits
Liver Extracts
Proteins
Triticum
Salts

ASJC Scopus subject areas

  • Biochemistry

Cite this

Ribosomal subunit antiassociation activity in rabbit reticulocyte lysates. Evidence for a low molecular weight ribosomal subunit antiassociation protein factor (M(r) = 25,000). / Raychaudhuri, P.; Stringer, E. A.; Valenzuela, D. M.; Maitra, U.

In: Journal of Biological Chemistry, Vol. 259, No. 19, 1984, p. 11930-11935.

Research output: Contribution to journalArticle

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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.",
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