
On the Mechanism of Interaction of N ‐Acetylphenylalanyl‐tRNA Phe with Ribosomes of Escherichia coli
Author(s) -
IVANOV Yuri V.,
GRAJEVSKAJA Rosa A.,
SAMINSKY Eugen M.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05085.x
Subject(s) - escherichia coli , ribosome , transfer rna , mechanism (biology) , chemistry , stereochemistry , physics , biochemistry , rna , gene , quantum mechanics
The tetranucleotide TpΨpCpGp acts as a specific inhibitor of the rate of AcPhe‐tRNA Phe binding in the ribosomal P site. This effect is observed both in the presence and in the absence of poly(U). In the absence of poly(U) antibiotics tetracycline and puromycin also decrease the rate of AcPhe‐tRNA Phe binding. Some inhibition by tetracycline is observed with poly(U). All these inhibitors are known to be ligands of the ribosomal A site, and their influence on the P site binding can be most naturally explained by the suggestion that AcPhe‐tRNA Phe enters the ribosome via the A site, forms there an intermediate complex, and spontaneous translocation into the P site follows. In the presence of poly(U) arguments in favour of this hypothesis are much weaker, but the same sequence of events is possible.