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 language||English (US)|
|Number of pages||8|
|Journal||Journal of Biological Chemistry|
|Publication status||Published - Jul 10 1982|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology