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Site-directed modification of the adenylation domain of the fusaricidin nonribosomal peptide synthetase for enhanced production of fusaricidin analogs

Authors
Han, Jae WooKim, Eun YoungLee, Jung MinKim, Yun SungBang, EunjungKim, Beom Seok
Issue Date
7월-2012
Publisher
SPRINGER
Keywords
Adenylation domain; Fusaricidin analogs; Non-ribosomal peptide synthetase; Paenibacillus polymyxa; Site-directed mutagenesis
Citation
BIOTECHNOLOGY LETTERS, v.34, no.7, pp.1327 - 1334
Indexed
SCIE
SCOPUS
Journal Title
BIOTECHNOLOGY LETTERS
Volume
34
Number
7
Start Page
1327
End Page
1334
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/107965
DOI
10.1007/s10529-012-0913-8
ISSN
0141-5492
Abstract
Fusaricidins produced by Paenibacillus polymyxa DBB1709 are lipopeptide antibiotics active against fungi and Gram-positive bacteria. The cyclic hexapeptide structures of fusaricidins are synthesized by fusaricidin synthetase, a non-ribosomal peptide synthetase. The adenylation domain of the third module (FusA-A3) can recruit l-Tyr, l-Val, l-Ile, l-allo-Ile, or l-Phe, which diversifies the fusaricidin structures. Since the l-Phe-incorporated fusaricidin analog (LI-F07) exhibits more potent antimicrobial activity than other analogs, we modified a specificity-conferring sequence in the substrate binding pocket of FusA-A3 to direct the enhanced production of LI-F07. Base on comparison to the adenylation domain of gramicidin S synthetase 1 and tyrocidine synthetase 1, both of which mainly activate l-Phe, six mutant strains with altered FusA-A3 were generated using site-directed mutagenesis. M3 (I239W, I299V), M5 (I299V, G322A, V330I), and M6 (S239W, I299V, G322A, V330I) mutants produced significantly more LI-F07 than the wild-type strain.
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