Eukaryotic ribosomal subunit anti-association activity of calf liver is contained in a single polypeptide chain protein of Mr = 25,500 (eukaryotic initiation factor 6).

D. M. Valenzuela, A. Chaudhuri, U. Maitra

Research output: Contribution to journalArticle

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Abstract

A protein factor that prevents the reassociation of eukaryotic 40 S and 60 S ribosomal subunits when the Mg+ concentration is raised from 1 to 5 mM has been purified to apparent electrophoretic homogeneity from postribosomal supernatant of calf liver extracts. The purified ribosomal subunit anti-association factor is a relatively heat-sensitive protein consisting of a single polypeptide chain of apparent Mr = 25,500. Direct assay for ribosomal subunit anti-association activity indicates that the majority (greater than 90% of such an activity in calf liver extracts can be accounted for by the presence of this 25,500-dalton protein factor in the postribosomal supernatant. The ribosomal salt wash protein fractions are virtually devoid of any significant ribosomal subunit anti-association or 80 S ribosome dissociation activity. The purified anti-association factor maintains a pool of ribosomal subunits by binding to 60 S ribosomal subunits and preventing them from reassociating with 40 S ribosomal subunits, rather than by dissociating 80 S monosomes. The factor neither binds to, nor seems to interact directly with, 40 S subunits. The properties of this factor are thus similar to wheat germ ribosome dissociation factor (eukaryotic initiation factor 6) described by Russell and Spremulli ((1979) J. Biol. Chem. 254, 8796-8800.

Original languageEnglish (US)
Pages (from-to)7712-7719
Number of pages8
JournalJournal of Biological Chemistry
Volume257
Issue number13
StatePublished - Jul 10 1982
Externally publishedYes

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Ribosome Subunits
Liver
Association reactions
Liver Extracts
Peptides
Proteins
Ribosomes
Assays
Thermodynamic properties
Salts
eIF-6
Triticum
Hot Temperature

ASJC Scopus subject areas

  • Biochemistry

Cite this

Eukaryotic ribosomal subunit anti-association activity of calf liver is contained in a single polypeptide chain protein of Mr = 25,500 (eukaryotic initiation factor 6). / Valenzuela, D. M.; Chaudhuri, A.; Maitra, U.

In: Journal of Biological Chemistry, Vol. 257, No. 13, 10.07.1982, p. 7712-7719.

Research output: Contribution to journalArticle

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abstract = "A protein factor that prevents the reassociation of eukaryotic 40 S and 60 S ribosomal subunits when the Mg+ concentration is raised from 1 to 5 mM has been purified to apparent electrophoretic homogeneity from postribosomal supernatant of calf liver extracts. The purified ribosomal subunit anti-association factor is a relatively heat-sensitive protein consisting of a single polypeptide chain of apparent Mr = 25,500. Direct assay for ribosomal subunit anti-association activity indicates that the majority (greater than 90{\%} of such an activity in calf liver extracts can be accounted for by the presence of this 25,500-dalton protein factor in the postribosomal supernatant. The ribosomal salt wash protein fractions are virtually devoid of any significant ribosomal subunit anti-association or 80 S ribosome dissociation activity. The purified anti-association factor maintains a pool of ribosomal subunits by binding to 60 S ribosomal subunits and preventing them from reassociating with 40 S ribosomal subunits, rather than by dissociating 80 S monosomes. The factor neither binds to, nor seems to interact directly with, 40 S subunits. The properties of this factor are thus similar to wheat germ ribosome dissociation factor (eukaryotic initiation factor 6) described by Russell and Spremulli ((1979) J. Biol. Chem. 254, 8796-8800.",
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