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Affinity labelling of Escherichia coli ribosomes with a benzylidene derivative of AUGU 6 within initiation and pretranslocational complexes
Author(s) -
Babkina G.T.,
Veniaminova A.G.,
Vladimirov S.N.,
Karpova G.G.,
Yamkovoy V.I.,
Berzin V.A.,
Gren E.J.,
Cielens I.E.
Publication year - 1986
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(86)80714-1
Subject(s) - ribosome , ternary complex , gtp' , start codon , labelling , 30s , escherichia coli , biochemistry , chemistry , stereochemistry , 50s , ribosomal rna , derivative (finance) , ef tu , eukaryotic ribosome , affinity labeling , complex formation , biology , rna , binding site , nucleotide , enzyme , gene , inorganic chemistry , financial economics , economics
Affinity labelling of E. coli ribosomes with the 2',3'‐ O ‐[4‐( N ‐2‐chloroethyl)‐ N ‐methylamino]benzylidene derivative of AUGU 6 was studied within the initiation complex (complex I) obtained by using fMet‐tRNA f Met and initiation factors and within the pretranslocational complex (complex II) obtained by treatment of complex I with the ternary complex Phe‐tRNA Phe ‐GTP‐EF‐Tu. Both proteins and rRNA of 30 S as well as 50 S subunits were found to be labelled. Sets of proteins labelled within complexes I and II differ considerably. Within complex II, proteins S13 and L10 were labelled preferentially. On the other hand, within complex I, multiple modification is observed (proteins S4, S12, S13, S14, S15, S18, S19, S20/L26 were found to be alkylated) despite the single fixation of a template in the ribosome by interaction of the AUG codon with fMet‐tRNA f Met .