An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center

Naohiro Terasaka; Gosuke Hayashi; Takayuki Katoh; Hiroaki Suga

doi:10.1038/nchembio.1549

An orthogonal ribosome-tRNA pair via engineering of the peptidyl transferase center

Nat Chem Biol. 2014 Jul;10(7):555-7. doi: 10.1038/nchembio.1549. Epub 2014 Jun 8.

Authors

Naohiro Terasaka¹, Gosuke Hayashi², Takayuki Katoh³, Hiroaki Suga⁴

Affiliations

¹ 1] Department of Chemistry, Graduate School of Science, University of Tokyo, Tokyo, Japan. [2].
² 1] Department of Chemistry, Graduate School of Science, University of Tokyo, Tokyo, Japan. [2] [3].
³ Department of Chemistry, Graduate School of Science, University of Tokyo, Tokyo, Japan.
⁴ 1] Department of Chemistry, Graduate School of Science, University of Tokyo, Tokyo, Japan. [2] Japan Science and Technology Agency, Core Research for Evolutional Science and Technology, University of Tokyo, Tokyo, Japan.

PMID: 24907900
DOI: 10.1038/nchembio.1549

Abstract

The Watson-Crick base pairs between the 3'-terminal end of tRNAs and ribosomal RNA in the peptidyl transferase center are universally conserved. Here, we report that the introduction of compensatory mutations to Escherichia coli RNAs in this site leads to an orthogonal system independent of the wild-type counterpart, as demonstrated via the production of two peptide sequences from a single mRNA. This work thus identifies a new way to reprogram the genetic code.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Base Pairing
Escherichia coli / genetics*
Escherichia coli / metabolism
Escherichia coli Proteins / genetics*
Escherichia coli Proteins / metabolism
Genetic Code
Mutation
Peptidyl Transferases / genetics*
Peptidyl Transferases / metabolism
Protein Biosynthesis*
Protein Engineering
RNA, Ribosomal, 23S / genetics*
RNA, Ribosomal, 23S / metabolism
RNA, Transfer / genetics*
RNA, Transfer / metabolism
Ribosomes / genetics
Ribosomes / metabolism

Substances

Escherichia coli Proteins
RNA, Ribosomal, 23S
RNA, Transfer
Peptidyl Transferases

Associated data

PubChem-Substance/178633619