AI Article Synopsis
- Tripartite efflux systems, like PvdRT-OpmQ, play a role in transporting substances and contributing to antibiotic resistance in Gram-negative bacteria.
- PvdT and PvdR are key components of the PvdRT system in Pseudomonas putida KT2440, with PvdT exhibiting ATPase activity boosted by PvdR.
- The study offers the first biochemical proof of direct interactions between the substrate pyoverdine and the PvdRT system.
Article Abstract
Tripartite efflux systems of the ABC-type family transport a variety of substrates and contribute to the antimicrobial resistance of Gram-negative bacteria. PvdRT-OpmQ, a member of this family, is thought to be involved in the secretion of the newly synthesized and recycled siderophore pyoverdine in Pseudomonas species. Here, we purified and characterized the inner membrane component PvdT and the periplasmic adapter protein PvdR of the plant growth-promoting soil bacterium Pseudomonas putida KT2440. We show that PvdT possesses an ATPase activity that is stimulated by the addition of PvdR. In addition, we provide the first biochemical evidence for direct interactions between pyoverdine and PvdRT.
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| http://dx.doi.org/10.1002/1873-3468.14601 | DOI Listing |
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