Role of Two Exceptional trans Adenylation Domains and MbtH‐like Proteins in the Biosynthesis of the Nonribosomal Peptide WS9324A from Streptomyces calvus ATCC 13382

Abstract: Nonribosomal peptide synthetases (NRPS) are organized in a modular arrangement. Usually, the modular order corresponds to the assembly of the amino acids in the respective peptide, following the collinearity rule. The WS9326A biosynthetic gene cluster from Streptomyces calvus shows deviations from this rule. Most interesting is the presence of two trans adenylation domains that are located downstream of the modular NRPS arrangement. Adenylation domains are responsible for the activation of their respective amino acids. In this study, we confirmed the involvement of the trans adenylation domains in WS9326A biosynthesis by performing gene knockout experiments and by observing the selective adenylation of their predicted amino acid substrates in vitro. We conclude that the trans adenylation domains are essential for WS9326A biosynthesis. Moreover, both adenylation domains are observed to have MbtH‐like protein dependency. Overall, we conclude that the trans adenylation domains are essential for WS9326A biosynthesis.

Standort
Deutsche Nationalbibliothek Frankfurt am Main
Umfang
Online-Ressource
Sprache
Englisch

Erschienen in
Role of Two Exceptional trans Adenylation Domains and MbtH‐like Proteins in the Biosynthesis of the Nonribosomal Peptide WS9324A from Streptomyces calvus ATCC 13382 ; volume:21 ; number:18 ; year:2020 ; pages:2659-2666 ; extent:8
ChemBioChem ; 21, Heft 18 (2020), 2659-2666 (gesamt 8)

Urheber
Bernhardt, Mirjam
Berman, Stefanie
Zechel, David
Bechthold, Andreas

DOI
10.1002/cbic.202000142
URN
urn:nbn:de:101:1-2022061805290587377667
Rechteinformation
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
Letzte Aktualisierung
15.08.2025, 07:25 MESZ

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