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The role of eIF-4C in protein synthesis initiation complex formation.

作者信息

Goumans H, Thomas A, Verhoeven A, Voorma H O, Benne R

出版信息

Biochim Biophys Acta. 1980 Jun 27;608(1):39-46. doi: 10.1016/0005-2787(80)90131-8.

DOI:10.1016/0005-2787(80)90131-8
PMID:6901506
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.

摘要

相似文献

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