Mirror-Image 5S Ribonucleoprotein Complexes
Journal article, 2020

After realizing mirror-image genetic replication, transcription, and reverse transcription, the biggest challenge in establishing a mirror-image version of the central dogma is to build a mirror-image ribosome-based translation machine. Here, we chemically synthesized the natural and mirror-image versions of three ribosomal proteins (L5, L18, and L25) in the large subunit of the Escherichia coli ribosome with post-translational modifications. We show that the synthetic mirror-image proteins can fold in vitro despite limited efficiency and assemble with enzymatically transcribed mirror-image 5S ribosomal RNA into ribonucleoprotein complexes. In addition, the RNA-protein interactions are chiral-specific in that the mirror-image ribosomal proteins do not bind with natural 5S ribosomal RNA and vice versa. The synthesis and assembly of mirror-image 5S ribonucleoprotein complexes are important steps towards building a functional mirror-image ribosome.

native chemical ligation

chirality

solid-phase peptide synthesis

ribonucleoproteins

chemical protein synthesis

Author

Jun-Jie Ling

Tsinghua University

Chuyao Fan

Tsinghua University

Hong Qin

Tsinghua University

Min Wang

Tsinghua University

Ji Chen

Tsinghua University

Pernilla Wittung Stafshede

Chalmers, Biology and Biological Engineering, Chemical Biology

Ting F. Zhu

Tsinghua University

Angewandte Chemie - International Edition

1433-7851 (ISSN) 1521-3773 (eISSN)

Vol. 59 9 3724-3731

Subject Categories

Biochemistry and Molecular Biology

Structural Biology

Computer Vision and Robotics (Autonomous Systems)

DOI

10.1002/anie.201914799

PubMed

31841243

More information

Latest update

4/23/2020