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Title of Journal: Amino Acids

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Abbravation: Amino Acids

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Springer Vienna

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DOI

10.1007/bf01665322

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ISSN

1438-2199

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Dual effect of chloramphenicol peptides on ribosom

Authors: Anthony Bougas Ioannis A Vlachogiannis Dimitrios Gatos Stefan Arenz George P Dinos
Publish Date: 2017/03/10
Volume: 49, Issue: 5, Pages: 995-1004
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Abstract

Chloramphenicol peptides were recently established as useful tools for probing nascent polypeptide chain interaction with the ribosome either biochemically or structurally Here we present a new 10mer chloramphenicol peptide which exerts a dual inhibition effect on the ribosome function affecting two distinct areas of the ribosome namely the peptidyl transferase center and the polypeptide exit tunnel According to our data the chloramphenicol peptide bound on the chloramphenicol binding site inhibits the formation of both acetylphenylalaninepuromycin and acetyllysinepuromycin showing however a decreased peptidyl transferase inhibition compared to chloramphenicolmediated inhibition per se Additionally we found that the same compound is a strong inhibitor of green fluorescent protein synthesis in a coupled in vitro transcriptiontranslation assay as well as a potent inhibitor of lysine polymerization in a polyAprogrammed ribosome showing that an additional inhibitory effect may exist Since chemical protection data supported the interaction of the antibiotic with bases A2058 and A2059 near the entrance of the tunnel we concluded that the extra inhibition effect on the synthesis of longer peptides is coming from interactions of the peptide moiety of the drug with residues comprising the ribosomal tunnel and by filling up the tunnel and blocking nascent chain progression through the restricted tunnel Therefore the dual interaction of the chloramphenicol peptide with the ribosome increases its inhibitory effect and opens a new window for improving the antimicrobial potency of classical antibiotics or designing new ones

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