Biopolymers and cell. 1989. Volume 5. № 1. 35 - 40
S. N. Vladimirov, D. M. Graifer, M. A. Zenkova, G. Y. Karpova, L. V. Olenina, S. V. Kirillov, E. M. Makarov, V. I. Makhno, Yu. P. Semenkov
PHOTOAFFINITY MODIFICATION OF E-SITE of Escherichia coli RIBOSOMES
Summary
Photoaffinity modification of E. coli ribosomes with tRNAphe derivative bearing arylazidogroups statistically scattered over guanine residues was studied under conditions of binding of the deacylated tRNAphe (tRNAoJ|) derivative at 70S ribosomal E-site (without template, in the presence of antibiotic edeine). Proteins S8, S15, S17, S18, S21 and L10 were found to be labelled. Another set of proteins — L2, L7/L12, L10, L16, L25 and L26 — was identified as being labelled within the complex of the tRNAOfj derivative with isolated SOS subunits.