Photoaffinity modification of E-site of Escherichia coli ribosomes

Vladimirov, S. N.; Graifer, D. M.; Zenkova, M. A.; Karpova, G. Y.; Olenina, L. V.; Kirillov, S. V.; Makarov, E. M.; Makhno, V. I.; Semenkov, Yu. P.

doi:10.7124/bc.000044

Biopolym. Cell. 1989; 5(1):35-40.

http://dx.doi.org/10.7124/bc.000044

Structure and Function of Biopolymers

Photoaffinity modification of E-site of Escherichia coli ribosomes

1Vladimirov S. N., 1Graifer D. M., 1Zenkova M. A., 1Karpova G. Y., 1Olenina L. V., 2Kirillov S. V., 2Makarov E. M., 2Makhno V. I., 2Semenkov Yu. P.

Institute of Bioorganic Chemistry, Siberian Branch of the Academy of Sciences of the USSR
Novosibirsk, USSR
B. P. Konstantinov Institute of Nuclear Physics, Academy of Sciences of the USSR
Gatchina, Leningrad distr., USSR

Abstract

Photoaffinity modification of E. coli ribosomes with tRNA^Phe derivative bearing arylazidogroups statistically scattered over guanine residues was studied under conditions of binding of the deacylated tRNAphe (tRNA^Phe) 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 tRNA^Phe derivative with isolated SOS subunits.

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