| Literature DB >> 2311763 |
E K Davydova1, L P Ovchinnikov.
Abstract
Elongation factor 2 (EF-2), ADP-ribosylated in vitro by the A-fragment of diphtheria toxin, can (in the presence of GMPPCP) form stable complexes with ribosomes regardless of whether the ribosomes are empty or carrying poly(U) and Phe-tRNA in the A-site. Despite its efficient binding to ribosomes, ADP-ribosyl-EF-2, in contrast to the non-modified EF-2 is unable to promote the shift of Phe-tRNA from the A-site to the P-site of the ribosome as determined by the puromycin reaction, i.e. it is incapable of promoting the translocation reaction within the ribosome.Entities:
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Year: 1990 PMID： 2311763 DOI： 10.1016/0014-5793(90)80589-b
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124