Ontology highlight
ABSTRACT:
SUBMITTER: Cheung-Lee WL
PROVIDER: S-EPMC7205569 | biostudies-literature | 2020 May
REPOSITORIES: biostudies-literature

Chembiochem : a European journal of chemical biology 20200103 9
We report the heterologous expression, structure, and antimicrobial activity of a lasso peptide, ubonodin, encoded in the genome of Burkholderia ubonensis. The topology of ubonodin is unprecedented amongst lasso peptides, with 18 of its 28 amino acids found in the mechanically bonded loop segment. Ubonodin inhibits RNA polymerase in vitro and has potent antimicrobial activity against several pathogenic members of the Burkholderia genus, most notably B. cepacia and B. multivorans, causative agent ...[more]