Open AccessInvolvement of both PKS and NRPS in antibacterial activity in Lysobacter enzymogenes OH 11
Author(s) -
Zhang Juan,
Du Liangcheng,
Liu Fengquan,
Xu Feifei,
Hu Baishi,
Venturi Vittorio,
Qian Guoliang
Publication year - 2014
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/1574-6968.12457
Subject(s) - nonribosomal peptide , gene cluster , polyketide synthase , biology , polyketide , gene , genome , genetics , microbiology and biotechnology , biosynthesis
Polyketides and nonribosomal peptides represent two large families of natural products ( NP s) with diverse structures and important functions. They are synthesized by polyketide synthase ( PKS ) and nonribosomal peptide synthetase ( NRPS ), respectively. Lysobacter enzymogenes is emerging as a novel biocontrol agent against pathogens of crop plants and a new source of bioactive NP s, such as antibacterial antibiotic WAP ‐8294A2 and antifungal antibiotic HSAF . Genome survey of strain OH 11, a Chinese L. enzymogenes isolate, detected four novel PKS , NRPS or hybrid gene clusters, designed as cluster A to D. We further individually mutated five genes ( PKS or NRPS ) located in these four gene clusters and showed that a PKS gene in cluster A and an NRPS gene in cluster D were involved in the antibacterial activity via a WAP ‐8294A2 dependent way. The data also showed that none of the five genes was associated with antifungal activity and the regulation of HSAF biosynthesis. Our results reveal the unusual regulatory role of these PKS and NRPS genes that were discovered from genome mining in L. enzymogenes .