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Deletion of com donor and acceptor domains and the interaction between modules in bacillomycin D produced by Bacillus amyloliquefaciens

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Synthetic and Systems Biotechnology 2022年第3期7卷 989-1001页

作者： Ziyan Lv Wenjie Ma Ping Zhang Zhaoxin Lu Libang Zhou Fanqiang Meng Zuwei Wang Xiaomei Bie Nanjing Agricultural University College of Food Science and TechnologyNanjing210095China

Bacillomycin D is a cyclic lipopeptide produced by Bacillus amyloliquefaciens *** present,no relevant report has described the combinatorial biosynthesis of bacillomycin *** to the strong biosynthetic potential of the communication-mediating(com)domains,its crosstalk between NRPS subunits has been studied to some extent,but the interaction of com domain between modules is rarely ***,in this study,we conducted the combinatorial biosynthesis of bacillomycin D through the deletion of the com donor and acceptor domains between the modules and elucidated the interaction between the NRPS *** results showed that the deletion of the donor domain between modules 2 and 3 did not affect catalysis by upstream modules,but prevented downstream modules from catalysing the extension of the lipopeptide product,ultimately resulting in mutant complexes that could form linear dipeptides with the sequenceβ-NH_(2)***,the engineered hybrid bacillomycin D NRPSs lacking the donor domains between modules 3 and 4 and modules 6 and 7 could form multiple assembly lines that produced bacillomycin D and its analogs(linear tripeptides,cyclic hexapeptides and linear hexapeptides).In addition,all the acceptor domain deletion strains failed to produce bacillomycin D,only truncated peptides produced by module interruption(except for the acceptor domain deletion strains between modules 3 and 4,which also produced cyclic hexapeptides).In conclusion,deletion of the inter-module donor domains led to a more flexible hybrid biosynthetic system for the production of diverse peptide products;compared with the inter-subunit donor domain deletion strains that could only produce truncated peptides,the former had a greater biosynthetic ***,the acceptor domains between modules were an important part of module-module interactions and efficient communication within bacillomycin D synthetase.

关键词： Bacillomycin D com domain Interaction between modules Lipopeptide analogs

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Translocation of subunit PPSE in plipastatin synthase and synthesis of novel lipopeptides

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Synthetic and Systems Biotechnology 2022年第4期7卷 1173-1180页

作者： Ling Gao Wenjie Ma Zhaoxin Lu Jinzhi Han Zhi Ma Hongxia Liu Xiaomei Bie Nanjing Agricultural University College of Food Science and TechnologyNanjing210095China Jiangnan University The Key Laboratory of Industrial BiotechnologyWuxi214122China

Nonribosomal peptide synthase(NRPS)is a unique molecular assembly mechanism with high *** recombination is conducive to the development of novel ***,there are few reports on NRPS subunit recombination of plipastatin at *** this paper,plipastatin synthase was modified by the forward movement of subunit PPSE and the replacement of the communication-mediating(com)*** results showed that ppsABE,a new assembly line,could synthesize novel lipopeptides such as cycle pentapeptide(C16-18β-OHFA-E-O-cyclo(Y-T-I),and its antimicrobial activity against Rhizopus stolonifer and Staphylococcus aureus was better than that of ***,the reactivity of ppsABCE disappeared,but the substitution of com^(D)_(ppsC)/com^(A)_(ppsD) or com^(D)_(ppsD)/com^(A)_(ppsE) for com^(D)_(ppsC)/com^(A)_(ppsE) could restore its activity and conduct the biosynthesis of linear hexapeptide(C16-17β-OHFA-E-O-Y-T-E-A/V)and heptapeptide(C17-18β-OHFA-E-O-Y-T-E-A-I).Collectively,these findings indicated that the com donor domain at the C-terminus of PPSB could communicate with the com acceptor domain at the N-terminus of PPSE and that the compatible com domain is an important tool for communication between nonpartner ***,the integrity and selective compatibility of the com acceptor domain of subunit PPSE are essential to promote the interaction between PPSE and other *** work further complemented the rules of NRPS subunit recombination and provided a theoretical basis for the development of novel high-efficiency lipopeptides.

关键词： Plipastatin Subunit translocation com domain compatibility Antimicrobial activity Novel lipopeptides

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Substitution of the communication‑mediating domain and the interaction between modules in bacillomycin D produced by Bacillus amyloliquefaciens

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Systems Microbiology and Biomanufacturing 2023年第4期3卷 792-804页

作者： Ziyan Lv Wenjie Ma Zhaoxin Lu Ping Zhang Fengxia Lu Haizhen Zhao Xiaomei Bie College of Food Science and Technology Nanjing Agricultural UniversityNanjing 210095People’s Republic of China

Bacillomycin D is a nonribosomal peptide produced by Bacillus amyloliquefaciens *** this study,the biosynthesis of bacillomycin D was mediated by replacing the intermodule donor,acceptor,and communication-mediating(com)domain pairs and introducing the com domain between the surfactin *** the homologous donor and the com domain pair replacement strains eliminated the selective barrier of the original com domain pair to a certain extent,resulting in a more flexible hybrid biosynthesis system that provides simultaneous biosynthesis of different lipopeptide *** synthesis of bacillomycin D in the homologous acceptor replacement strains was barely *** com domains between the surfactin subunits cannot establish efficient communication between the bacillomycin D *** conclusion,the com domains compatibility between the bacillomycin D modules are extremely strong,and the conserved amino acid residues in the acceptor domain are an important part of module–module interactions and efficient communication during bacillomycin D synthesis.

关键词： Bacillomycin D com domain Surfactin Intermodule interaction Synthetase reprogramming

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