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• W1969907855 endingPage "691" @default.
• W1969907855 startingPage "687" @default.
• W1969907855 abstract "Abstract The major enzymatic activity of the ribosome is the catalysis of peptide bond formation. The active site – the peptidyl transferase center – is composed of ribosomal RNA (rRNA), and interactions between rRNA and the reactants, peptidyl-tRNA and aminoacyl-tRNA, are crucial for the reaction to proceed rapidly and efficiently. Here, we describe the influence of rRNA interactions with cytidine residues in A-site substrate analogs (C-puromycin or CC-puromycin), mimicking C74 and C75 of tRNA on the reaction. Base-pairing of C75 with G2553 of 23S rRNA accelerates peptide bond formation, presumably by stabilizing the peptidyl transferase center in its productive conformation. When C74 is also present in the substrate analog, the reaction is slowed down considerably, indicating a slow step in substrate binding to the active site, which limits the reaction rate. The tRNA-rRNA interactions lead to a robust reaction that is insensitive to pH changes or base substitutions in 23S rRNA at the active site of the ribosome." @default.
• W1969907855 created "2016-06-24" @default.
• W1969907855 creator A5028476493 @default.
• W1969907855 creator A5035464151 @default.
• W1969907855 date "2007-07-01" @default.
• W1969907855 modified "2023-09-26" @default.
• W1969907855 title "Importance of tRNA interactions with 23S rRNA for peptide bond formation on the ribosome: studies with substrate analogs" @default.
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• W1969907855 doi "https://doi.org/10.1515/bc.2007.077" @default.
• W1969907855 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/17570820" @default.
• W1969907855 hasPublicationYear "2007" @default.
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