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TitleDefects in the Assembly of Ribosomes Selected for β-Amino Acid Incorporation.
Journal, issue, pagesBiochemistry, Vol. 58, Issue 45, Page 4494-4504, Year 2019
Publish dateNov 12, 2019
AuthorsFred R Ward / Zoe L Watson / Omer Ad / Alanna Schepartz / Jamie H D Cate /
PubMed AbstractRibosome engineering has emerged as a promising field in synthetic biology, particularly concerning the production of new sequence-defined polymers. Mutant ribosomes have been developed that improve ...Ribosome engineering has emerged as a promising field in synthetic biology, particularly concerning the production of new sequence-defined polymers. Mutant ribosomes have been developed that improve the incorporation of several nonstandard monomers including d-amino acids, dipeptides, and β-amino acids into polypeptide chains. However, there remains little mechanistic understanding of how these ribosomes catalyze incorporation of these new substrates. Here, we probed the properties of a mutant ribosome-P7A7-evolved for better β-amino acid incorporation through biochemistry and cryo-electron microscopy. Although P7A7 is a functional ribosome , it is inactive , and assembles poorly into 70S ribosome complexes. Structural characterization revealed large regions of disorder in the peptidyltransferase center and nearby features, suggesting a defect in assembly. Comparison of RNA helix and ribosomal protein occupancy with other assembly intermediates revealed that P7A7 is stalled at a late stage in ribosome assembly, explaining its weak activity. These results highlight the importance of ensuring efficient ribosome assembly during ribosome engineering toward new catalytic abilities.
External linksBiochemistry / PubMed:31607123 / PubMed Central
MethodsEM (single particle)
Resolution3.11 - 3.2 Å
Structure data

EMDB-20853:
P7A7 ribosome large subunit
Method: EM (single particle) / Resolution: 3.11 Å

EMDB-20854:
E. coli large ribosomal subunit
Method: EM (single particle) / Resolution: 3.2 Å

Source
  • Escherichia coli (E. coli)

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