Outwitting EF-Tu and the ribosome: translation with d-amino acids | Zendy

John Achenbach | Zendy; Michael Jahnz | Zendy; Lucas Bethge | Zendy; Krisztina Paál | Zendy; Maria Jung | Zendy; Maja Schuster | Zendy; Renate Albrecht | Zendy; Florian Jarosch | Zendy; Knud H. Nierhaus | Zendy; Sven Klußmann | Zendy

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Outwitting EF-Tu and the ribosome: translation with d-amino acids

Author(s) -

John Achenbach,

Michael Jahnz,

Lucas Bethge,

Krisztina Paál,

Maria Jung,

Maja Schuster,

Renate Albrecht,

Florian Jarosch,

Knud H. Nierhaus,

Sven Klußmann

Publication year - 2015

Publication title -

nucleic acids research

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 9.008

H-Index - 537

eISSN - 1362-4954

pISSN - 0305-1048

DOI - 10.1093/nar/gkv566

Subject(s) - ribosome , biology , translation (biology) , ribosomal rna , protein biosynthesis , transfer rna , amino acid , elongation factor , biochemistry , ribosomal protein , ef tu , peptidyl transferase , in vitro , biophysics , messenger rna , rna , gene

Key components of the translational apparatus, i.e. ribosomes, elongation factor EF-Tu and most aminoacyl-tRNA synthetases, are stereoselective and prevent incorporation of d-amino acids (d-aa) into polypeptides. The rare appearance of d-aa in natural polypeptides arises from post-translational modifications or non-ribosomal synthesis. We introduce an in vitro translation system that enables single incorporation of 17 out of 18 tested d-aa into a polypeptide; incorporation of two or three successive d-aa was also observed in several cases. The system consists of wild-type components and d-aa are introduced via artificially charged, unmodified tRNA(Gly) that was selected according to the rules of 'thermodynamic compensation'. The results reveal an unexpected plasticity of the ribosomal peptidyltransferase center and thus shed new light on the mechanism of chiral discrimination during translation. Furthermore, ribosomal incorporation of d-aa into polypeptides may greatly expand the armamentarium of in vitro translation towards the identification of peptides and proteins with new properties and functions.

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