Affinity labelling of Escherichia coli ribosomes with a benzylidene derivative of AUGU6 within initiation and pretranslocational complexes

Affinity labelling of E. coli ribosomes with the 2',3'‐O‐[4‐(N‐2‐chloroethyl)‐N‐methylamino]benzylidene derivative of AUGU6 was studied within the initiation complex (complex I) obtained by using fMet‐tRNAf Met and initiation factors and within the pretranslocational complex (complex II) o...

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Veröffentlicht in:	FEBS letters 1986-07, Vol.202 (2), p.340-344
Hauptverfasser:	Babkina, G.T., Veniaminova, A.G., Vladimirov, S.N., Karpova, G.G., Yamkovoy, V.I., Berzin, V.A., Gren, E.J., Cielens, I.E.
Format:	Artikel
Sprache:	eng
Schlagworte:	Affinity labeling Affinity Labels - metabolism Binding Sites Biological and medical sciences Codon Electron Transport Complex II Escherichia coli - genetics Escherichia coli - metabolism Fundamental and applied biological sciences. Psychology Guanosine Triphosphate - metabolism Initiation complex Molecular and cellular biology Molecular genetics mRNA-binding site Multienzyme Complexes - metabolism Mustard Compounds NAD(P)H Dehydrogenase (Quinone) Oligonucleotide derivative Oxidoreductases - metabolism Peptide Chain Initiation, Translational Peptide Elongation Factor Tu - metabolism Pretranslocational complex Quinone Reductases - metabolism Ribosomal protein Ribosomal Proteins - metabolism Ribosome Ribosomes - metabolism RNA, Messenger - metabolism RNA, Transfer, Amino Acyl - metabolism Succinate Dehydrogenase - metabolism Translation. Translation factors. Protein processing
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Zusammenfassung:	Affinity labelling of E. coli ribosomes with the 2',3'‐O‐[4‐(N‐2‐chloroethyl)‐N‐methylamino]benzylidene derivative of AUGU6 was studied within the initiation complex (complex I) obtained by using fMet‐tRNAf Met and initiation factors and within the pretranslocational complex (complex II) obtained by treatment of complex I with the ternary complex Phe‐tRNAPhe‐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‐tRNAf Met.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(86)80714-1