PMID:18369182

Citation	Beringer, M (2008) Modulating the activity of the peptidyl transferase center of the ribosome. RNA 14:795-801
Abstract	The peptidyl transferase (PT) center of the ribosome catalyzes two nucleophilic reactions, peptide bond formation between aminoacylated tRNA substrates and, together with release factor, peptide release. Structure and function of the PT center are modulated by binding of aminoacyl-tRNA or release factor, thus providing the basis for the specificity of catalysis. Another way by which the function of the PT center is controlled is signaling from the peptide exit tunnel. The SecM nascent peptide induces ribosome stalling, presumably by inhibition of peptide bond formation. Similarly, the release factor-induced hydrolytic activity of the PT center can be suppressed by the TnaC nascent peptide contained in the exit tunnel. Thus, local and long-range conformational rearrangements can lead to changes in the reaction specificity and catalytic activity of the PT center.
Links	PubMed PMC2327356 Online version:10.1261/rna.980308
Keywords	Catalytic Domain/genetics; Escherichia coli/genetics; Escherichia coli/metabolism; Escherichia coli Proteins/metabolism; Hydrolysis; Models, Biological; Peptidyl Transferases/genetics; Peptidyl Transferases/metabolism; Ribosomes/enzymology; Ribosomes/metabolism; Signal Transduction; Transcription Factors/metabolism
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