
Structural characteristics and classfication of some tRNA‐binding sites of elongating Escherichia coli ribosome
Author(s) -
ABDURASHIDOVA Gulnara G.,
BASKAYEVA Irena O.,
CHERNYI Alexey A.,
KAMINIR Lev B.,
BUDOWSKY Edward I.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09838.x
Subject(s) - transfer rna , ribosome , t arm , ribosomal rna , shine dalgarno sequence , ribosomal protein , ef tu , chemistry , elongation factor , protein biosynthesis , ribosomal binding site , biology , biochemistry , rna , gene
Ultraviolet(254 nm)‐irradiation‐induced cross‐linkages in ribosomal complexes allowed identification of proteins in contact with tRNA at different elongation steps. Both the set and the ratio of cross‐linked proteins, i.e. the structural characteristics of the tRNA‐binding sites of the ribosome, were shown to depend strongly not only on the position of the mRNA codon with which tRNA interacts as a component of a ribosomal complex, but also on its functional state, i.e. on the elongation step. A new classification of tRNA‐binding sites of ribosome is suggested.