Abstract:
:Kalimantacin is an antimicrobial compound with strong antistaphylococcal activity that is produced by a hybrid trans-acyltransferase polyketide synthase/nonribosomal peptide synthetase system in Pseudomonas fluorescens BCCM_ID9359. We here present a systematic analysis of the substrate specificity of the glycine-incorporating adenylation domain from the kalimantacin biosynthetic assembly line by a targeted mutagenesis approach. The specificity-conferring code was adapted for use in Pseudomonas and mutated adenylation domain active site sequences were introduced in the kalimantacin gene cluster, using a newly adapted ligation independent cloning method. Antimicrobial activity screens and LC-MS analyses revealed that the production of the kalimantacin analogues in the mutated strains was abolished. These results support the idea that further insight in the specificity of downstream domains in nonribosomal peptide synthetases and polyketide synthases is required to efficiently engineer these strains in vivo.
journal_name
Microbiologyopenjournal_title
MicrobiologyOpenauthors
Uytterhoeven B,Appermans K,Song L,Masschelein J,Lathouwers T,Michiels CW,Lavigne Rdoi
10.1002/mbo3.326subject
Has Abstractpub_date
2016-04-01 00:00:00pages
279-86issue
2issn
2045-8827journal_volume
5pub_type
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