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The structure of helix 89 of 23S rRNA is important for peptidyl transferase function of Escherichia coli ribosome
Author(s) -
Burakovsky Dmitry E.,
Sergiev Petr V.,
Steblyanko Maria A.,
Konevega Andrey L.,
Bogdanov Alexey A.,
Dontsova Olga A.
Publication year - 2011
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/j.febslet.2011.08.030
Subject(s) - peptidyl transferase , 23s ribosomal rna , ribosome , ribosomal rna , helix (gastropod) , puromycin , protein secondary structure , mutagenesis , transfer rna , 50s , p site , mutant , chemistry , base pair , biology , protein biosynthesis , crystallography , biochemistry , rna , dna , ecology , snail , gene
Helix 89 of the 23S rRNA connects ribosomal peptidyltransferase center and elongation factor binding site. Secondary structure of helix 89 determined by X‐ray structural analysis involves less base pairs then could be drawn for the helix of the same primary structure. It can be that alternative secondary structure might be realized at some stage of translation. Here by means of site‐directed mutagenesis we stabilized either the “X‐ray” structure or the structure with largest number of paired nucleotides. Mutation UU2492‐3C which aimed to provide maximal pairing of the helix 89 of the 23S rRNA was lethal. Mutant ribosomes were unable to catalyze peptide transfer independently either with aminoacyl‐tRNA or puromycin.