Unknown

Dataset Information

0

Mirror-Image 5S Ribonucleoprotein Complexes.


ABSTRACT: 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.

SUBMITTER: Ling JJ 

PROVIDER: S-EPMC7217020 | biostudies-literature | 2020 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Mirror-Image 5S Ribonucleoprotein Complexes.

Ling Jun-Jie JJ   Fan Chuyao C   Qin Hong H   Wang Min M   Chen Ji J   Wittung-Stafshede Pernilla P   Zhu Ting F TF  

Angewandte Chemie (International ed. in English) 20200121 9


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  ...[more]

Similar Datasets

| S-EPMC4201793 | biostudies-other
| S-EPMC5643884 | biostudies-literature
2024-01-19 | PXD046228 | Pride
| S-EPMC4905334 | biostudies-other
| S-EPMC5492103 | biostudies-literature
| S-EPMC3281068 | biostudies-literature
| S-EPMC1134106 | biostudies-literature