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Rapid peptide bond formation on isolated 50S ribosomal subunits
Author(s) -
Wohlgemuth Ingo,
Beringer Malte,
Rodnina Marina V
Publication year - 2006
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/sj.embor.7400732
Subject(s) - 50s , peptidyl transferase , ribosome , puromycin , ribosomal rna , peptide bond , transfer rna , chemistry , eukaryotic ribosome , p site , eukaryotic large ribosomal subunit , protein subunit , peptide biosynthesis , biochemistry , 30s , peptide , biology , stereochemistry , rna , protein biosynthesis , gene
The catalytic site of the ribosome, the peptidyl transferase centre, is located on the large (50S in bacteria) ribosomal subunit. On the basis of results obtained with small substrate analogues, isolated 50S subunits seem to be less active in peptide bond formation than 70S ribosomes by several orders of magnitude, suggesting that the reaction mechanisms on 50S subunits and 70S ribosomes may be different. Here we show that with full‐size fMet‐tRNA fMet and puromycin or C‐puromycin as peptide donor and acceptor substrates, respectively, the reaction proceeds as rapidly on 50S subunits as on 70S ribosomes, indicating that the intrinsic activity of 50S subunits is not different from that of 70S ribosomes. The faster reaction on 50S subunits with fMet‐tRNA fMet , compared with oligonucleotide substrate analogues, suggests that full‐size transfer RNA in the P site is important for maintaining the active conformation of the peptidyl transferase centre.