PDF(Pubmed)
Abstract：
The pyoverdine siderophore is produced by Pseudomonas aeruginosa to access iron. Its synthesis involves the complex coordination of four nonribosomal peptide synthetases (NRPSs), which are responsible for assembling the pyoverdine peptide backbone. The precise cellular organization of these NRPSs and their mechanisms of interaction remain unclear. Here, we used a combination of several single-molecule microscopy techniques to elucidate the spatial arrangement of NRPSs within pyoverdine-producing cells. Our findings reveal that PvdL differs from the three other NRPSs in terms of localization and mobility patterns. PvdL is predominantly located in the inner membrane, while the others also explore the cytoplasmic compartment. Leveraging the power of multicolor single-molecule localization, we further reveal co-localization between PvdL and the other NRPSs, suggesting a pivotal role for PvdL in orchestrating the intricate biosynthetic pathway. Our observations strongly indicates that PvdL serves as a central orchestrator in the assembly of NRPSs involved in pyoverdine biosynthesis, assuming a critical regulatory function.
摘要：
铜绿假单胞菌产生铜绿铁载体以获取铁。它的合成涉及四种非核糖体肽合成酶（NRPS）的复杂协调，负责组装pyoverdine肽骨架。这些NRPS的精确细胞组织及其相互作用机制仍不清楚。这里,我们使用了几种单分子显微镜技术的组合来阐明NRPSs在产生pyoverdine的细胞内的空间排列.我们的发现表明，PvdL在定位和迁移模式方面与其他三个NRPS不同。PvdL主要位于内膜，而其他人也探索细胞质区室。利用多色单分子定位的力量，我们进一步揭示了PvdL和其他NRPS之间的共定位，提示PvdL在协调复杂的生物合成途径中的关键作用。我们的观察强烈表明，PvdL在参与pyoverdine生物合成的NRPS组装中充当中心协调器，假设关键的调节功能。
