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Original article (peer-reviewed)

Journal BMC BIOCHEMISTRY
Volume (Issue) 10(26)
Page(s) 1 - 9
Title of proceedings BMC BIOCHEMISTRY
DOI 10.1186/1471-2091-10-26

Open Access

URL http://www.zora.uzh.ch/23752/2/Ramel_et_al_BMC.pdf
Type of Open Access Repository (Green Open Access)

Abstract

Syringolin A, an important virulence factor in the interaction of the phytopathogenic bacterium Pseudomonas syringae pv. syringae B728a with its host plant Phaseolus vulgaris (bean), was recently shown to irreversibly inhibit eukaryotic proteasomes by a novel mechanism. Syringolin A is synthesized by a mixed non-ribosomal peptide synthetase/polyketide synthetase and consists of a tripeptide part including a twelve-membered ring with an N-terminal valine that is joined to a second valine via a very unusual ureido group. Analysis of sequence and architecture of the syringolin A synthetase gene cluster with the five open reading frames sylA-sylE allowed to formulate a biosynthesis model that explained all structural features of the tripeptide part of syringolin A but left the biosynthesis of the unusual ureido group unaccounted for.
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