Alexander S. Mankin

University of Illinois Chicago

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Nora Vázquez‐Laslop

University of Illinois Chicago

Dorota Klepacki

University of Illinois Chicago

Yury S. Polikanov

University of Illinois Chicago

Liqun Xiong

University of Illinois Chicago

Jamie H. D. Cate

University of California, Berkeley

J.A. Dunkle

University of Alabama

V.K. Kagramanova

Lomonosov Moscow State University

L. Xiong

Chengdu Women's and Children's Central Hospital

Tanel Tenson

University of Tartu

Haripriya Ramu

AstraZeneca (United Kingdom)

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University of Illinois Chicago

120

Lancaster City Council

108

Lomonosov Moscow State University

Harvard University

Ashland (United States)

Howard Hughes Medical Institute

Centre National de la Recherche Scientifique

Weatherford College

National Institutes of Health

University of California, San Francisco

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A fully orthogonal system for protein synthesis in bacterial cells

Nature Communications (2020)

Nikolay A. Aleksashin Teresa Szal Anne E. d’Aquino Michael C. Jewett Nora Vázquez‐Laslop

Abstract Ribosome engineering is a powerful approach for expanding the catalytic potential of the protein synthesis apparatus. Due to the potential detriment the properties of the engineered ribosome may have on the cell, the designer ribosome needs to be functionally isolated from the translation machinery synthesizing cellular proteins. One solution to this problem was offered by Ribo-T, an engineered ribosome with tethered subunits which, while producing a desired protein, could be excluded from general translation. Here, we provide a conceptually different design of a cell with two orthogonal protein synthesis systems, where Ribo-T produces the proteome, while the dissociable ribosome is committed to the translation of a specific mRNA. The utility of this system is illustrated by generating a comprehensive collection of mutants with alterations at every rRNA nucleotide of the peptidyl transferase center and isolating gain-of-function variants that enable the ribosome to overcome the translation termination blockage imposed by an arrest peptide.

Peptidyl transferase

Ribosome profiling

Proteome

10.1038/s41467-020-15756-1

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Citations (49)

Dynamics of the context-specific translation arrest by chloramphenicol and linezolid

Nature Chemical Biology (2019)

Junhong Choi James Marks Jingji Zhang Dong-Hua Chen Jinfan Wang

Peptide bond

10.1038/s41589-019-0423-2

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