Document Detail


Target profiling of 4-hydroxyderricin in S. aureus reveals seryl-tRNA synthetase binding and inhibition by covalent modification.
MedLine Citation:
PMID:  23295910     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
4-Hydroxyderricin is a heat labile bioactive chalcone isolated from the plant Angelica keiskei. It received attention due to its antibiotic potency against several strains of bacteria including pathogens such as Staphylococcus aureus. Despite these promising pharmacological properties, the exact mode of action or the biological targets are still unknown. Here we report the synthesis and the application of a 4-hydroxyderricin probe for activity-based protein profiling (ABPP) in S. aureus. Due to the heat sensitivity of the natural product we utilize a chemical tool for the mild and selective enrichment of labile probe-protein conjugates and report seryl-tRNA synthetase (STS) to be covalently modified by our probe. This modification results in inhibition of the amino acylation of tRNAs catalyzed by S. aureus STS which is an essential enzymatic pathway for bacterial viability.
Authors:
Oliver A Battenberg; Yinliang Yang; Steven H L Verhelst; Stephan A Sieber
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-8
Journal Detail:
Title:  Molecular bioSystems     Volume:  -     ISSN:  1742-2051     ISO Abbreviation:  Mol Biosyst     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-8     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101251620     Medline TA:  Mol Biosyst     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
Affiliation:
Center for Integrated Protein Science Munich (CIPSM), Lehrstuhl für organische Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany. stephan.sieber@tum.de.
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