ArticleCommunications biology2026
Multiple active-sites editing of adenylation domains of srfA operon for constructing diverse surfactin lipopeptide.
Article in Communications biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
The srfA operon, which encodes the surfactin synthase SrfA in Bacillus rhizobacteria, is essential for surfactin biosynthesis. As a typical non-ribosomal peptide synthetase (NRPS), the adenylation domain of SrfA determines the structure of the synthesized peptide. A major challenge in the field lies in the precise and efficient engineering of NRPS adenylation domains to generate diverse surfactin variants with enhanced bioactivities. Herein, we applied a non-specific guide RNA system (UgRNA/Cas9) for multi-site and diversified editing of the srfA operon in the high-secreting strain Bacillus pumilus LG3145. UgRNAs targeting four conserved motifs around the SrfA active pocket were designed to direct Cas9-mediated replacement of Stachelhaus codes with codons for 28 different amino acids. This strategy generated two engineered strains: WA1, which carries a Val→Phe mutation in module 2 and produces [Ser
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