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Evolutionarily conserved binding of ribosomes to the translocation channel via the large ribosomal RNA
Author(s) -
Prinz Anke,
Behrens Christina,
Rapoport Tom A.,
Hartmann Enno,
Kalies KaiUwe
Publication year - 2000
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1093/emboj/19.8.1900
Subject(s) - ribosome , biology , eukaryotic small ribosomal subunit , translocon , eukaryotic ribosome , ribosomal rna , 23s ribosomal rna , eukaryotic large ribosomal subunit , ribosomal protein , microbiology and biotechnology , endoplasmic reticulum , rna , biochemistry , chromosomal translocation , gene
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.