Ribosome-catalyzed peptide-bond formation with an A-site substrate covalently linked to 23S ribosomal RNA

Rachel Green, Christopher Switzer, Harry F. Noller

Research output: Contribution to journalArticlepeer-review

Abstract

In the ribosome, the aminoacyl-transfer RNA (tRNA) analog 4-thio-dT-p- C-p-puromycin crosslinks photochemically with G2553 of 23S ribosomal RNA (rRNA). This covalently linked substrate reacts with a peptidyl-tRNA analog to form a peptide bond in a peptidyl transferase-catalyzed reaction. This result places the conserved 2555 loop of 23S rRNA at the peptidyl transferase A site and suggests that peptide bond formation can occur uncoupled from movement of the A-site tRNA. Crosslink formation depends on occupancy of the P site by a tRNA carrying an intact CCA acceptor end, indicating that peptidyl-tRNA, directly or indirectly, helps to create the peptidyl transferase A site.

Original languageEnglish (US)
Pages (from-to)286-289
Number of pages4
JournalScience
Volume280
Issue number5361
DOIs
StatePublished - Apr 10 1998

ASJC Scopus subject areas

  • General

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