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Updated: Aug 14, 2026

Dual DNA Rulers to Study the Mechanism of Ribosome Translocation with Single-Nucleotide Resolution
Published on: July 8, 2019
Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
A Prinz1, C Behrens, T A Rapoport
1Abteilung Biochemie II, Zentrum Biochemie und Molekulare Zellbiologie, Georg-August-Universität, Heinrich-Düker-Weg 12, 37073 Göttingen, Germany.
Abstract:
During early stages of cotranslational protein translocation across the endoplasmic reticulum (ER) membrane the ribosome is targeted to the heterotrimeric Sec61p complex, the major component of the protein-conducting channel. We demonstrate that this interaction is mediated by the 28S rRNA of the eukaryotic large ribosomal subunit. Bacterial ribosomes also bind via their 23S rRNA to the bacterial homolog of the Sec61p complex, the SecYEG complex. Eukaryotic ribosomes bind to the SecYEG complex, and prokaryotic ribosomes to the Sec61p complex. These data indicate that rRNA-mediated interaction of ribosomes with the translocation channel occurred early in evolution and has been conserved.
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