Journal
CHEMBIOCHEM
Volume 23, Issue 14, Pages -Publisher
WILEY-V C H VERLAG GMBH
DOI: 10.1002/cbic.202200200
Keywords
acyl carrier protein; biosynthesis; ketosynthases; polyketide synthases; protein-protein interactions
Funding
- Japan Society for the Promotion of Science [20H02911, 20J13080]
- Ministry of Education, Culture, Sports, Science, and Technology (MEXT) [16H06451]
- Grants-in-Aid for Scientific Research [20H02911, 20J13080] Funding Source: KAKEN
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The ketosynthase (KS) domain is a critical component in polyketide synthases (PKSs) and plays a crucial role in the synthesis of polyketides. This study demonstrates the importance of protein-protein recognition in intermodular transacylation, highlighting its significance in modular PKSs.
The ketosynthase (KS) domain is a core domain found in modular polyketide synthases (PKSs). To maintain the polyketide biosynthetic fidelity, the KS domain must only accept an acyl group from the acyl carrier protein (ACP) domain of the immediate upstream module even when they are separated into different polypeptides. Although it was reported that both the docking domain-based interactions and KS-ACP compatibility are important for the interpolypeptide transacylation reaction in 6-deoxyerythronolide B synthase, it is not clear whether these findings are broadly applied to other modular PKSs. Herein, we describe the importance of protein-protein recognition in the intermodular transacylation between VinP1 module 3 and VinP2 module 4 in vicenistatin biosynthesis. We compared the transacylation activity and crosslinking efficiency of VinP2 KS4 against the cognate VinP1 ACP(3) with the noncognate one. As a result, it appeared that VinP2 KS4 distinguishes the cognate ACP(3) from other ACPs.
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