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Molecular insights into protein synthesis with proline residues

Lookup NU author(s): Dr Sergey MelnikovORCiD


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© 2016 The AuthorsProline is an amino acid with a unique cyclic structure that facilitates the folding of many proteins, but also impedes the rate of peptide bond formation by the ribosome. As a ribosome substrate, proline reacts markedly slower when compared with other amino acids both as a donor and as an acceptor of the nascent peptide. Furthermore, synthesis of peptides with consecutive proline residues triggers ribosome stalling. Here, we report crystal structures of the eukaryotic ribosome bound to analogs of mono- and diprolyl-tRNAs. These structures provide a high-resolution insight into unique properties of proline as a ribosome substrate. They show that the cyclic structure of proline residue prevents proline positioning in the amino acid binding pocket and affects the nascent peptide chain position in the ribosomal peptide exit tunnel. These observations extend current knowledge of the protein synthesis mechanism. They also revise an old dogma that amino acids bind the ribosomal active site in a uniform way by showing that proline has a binding mode distinct from other amino acids.

Publication metadata

Author(s): Melnikov S, Mailliot J, Rigger L, Neuner S, Shin B-S, Yusupova G, Dever TE, Micura R, Yusupov M

Publication type: Article

Publication status: Published

Journal: EMBO Reports

Year: 2016

Volume: 17

Issue: 12

Pages: 1776-1784

Print publication date: 01/12/2016

Online publication date: 08/11/2016

Acceptance date: 30/09/2016

ISSN (print): 1469-221X

ISSN (electronic): 1469-3178

Publisher: Wiley-VCH Verlag


DOI: 10.15252/embr.201642943

PubMed id: 27827794


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