Abstract
eIF-4C has a pronounced stimulatory effect on initiation complex formation with native 80-S ribosomes (80-Sn) as the only source of ribosomal subunits, but only a small effect when washed 40-S subunits are used. eIF-4C is accessary to eIF-3 in dissociating 80-Sn ribosomes. eIF-4C is present on 40-Sn but absent on 40-Sn dimers, which occur in preparations of native ribosomes and are as such inactive in protein synthesis. eIF-4C dissociates 40-Sn dimers into active monomers. These results can be explained by assuming that the presence of eIF-4C on 40-Sn prevents: (a) premature association with 60-S ribosomal subunits and (b) dimerisation, thus increasing the rate and extent of initiation complex formation.
| Original language | English |
|---|---|
| Pages (from-to) | 39-46 |
| Number of pages | 8 |
| Journal | Biochimica et Biophysica Acta |
| Volume | 608 |
| Issue number | 1 |
| Publication status | Published - 27 Jun 1980 |
Keywords
- Animals
- Eukaryotic Initiation Factor-1
- Kinetics
- Macromolecular Substances
- Molecular Weight
- Peptide Chain Initiation, Translational
- Peptide Initiation Factors
- RNA, Transfer, Amino Acyl
- Rabbits
- Ribosomal Proteins
- Ribosomes
- Tritium