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The effect of GTP hydrolysis and transpeptidation on the arrangement of aminoacyl‐tRNA at the A‐site of Escherichia coli 70 S ribosomes
Author(s) -
Vladimirov S.N.,
Graifer D.M.,
Karpova G.G.,
Semenkov Yu.P.,
Makhno V.I.,
Kirillov S.V.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80294-5
Subject(s) - gtp' , ribosome , aminoacyl trna , transfer rna , gtpase , biochemistry , hydrolysis , chemistry , escherichia coli , ribosomal protein , biology , rna , enzyme , gene
From the affinity labelling of 70 S ribosomes with a photoreactive derivative of Phe‐tRNA phe bearing an arylazido group on guanine residues, it has been found that different sets of ribosomal proteins are labelled in the course of three successive steps of EF‐Tu‐dependent binding of aminoacyl‐tRNA derivative at the A‐site. Proteins S5, S7, S8, S16, S17, L9, L14, L15 and L24 were labelled before GTP hydrolysis; proteins S5, S7, S9, S11, S14, S18, S19, S21, L9, L21 and L29 ‐ after GTP hydrolysis; proteins S2, S5, S7, S21, L11 and L23 ‐ after GTP hydrolysis and transpeptidation.