The ABC transporter family efflux pump PvdRT-OpmQ of Pseudomonas putida KT2440: purification and initial characterization

被引:3
作者
Stein, Nicola Victoria [1 ]
Eder, Michelle [1 ]
Brameyer, Sophie [1 ,2 ]
Schwenkert, Serena [3 ]
Jung, Heinrich [1 ,4 ]
机构
[1] Ludwig Maximilians Univ Munchen, Fac Biol, Microbiol, Martinsried, Germany
[2] Ludwig Maximilians Univ Munchen, Fac Biol, Serv Unit Bioanalyt, Martinsried, Germany
[3] Ludwig Maximilians Univ Munchen, Fac Biol, Serv Unit Mass Spectrometry Biomol, Martinsried, Germany
[4] Ludwig Maximilians Univ Munchen, Fac Biol, Div Microbiol, Martinsried, Germany
关键词
ABC transporter; ligand binding; membrane protein purification; pyoverdine; siderophore; tripartite efflux pump; ATPASE ACTIVITY; PROTEIN; SIDEROPHORE; BIOSYNTHESIS; SECRETION; BINDING; ASSAY;
D O I
10.1002/1873-3468.14601
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:1403 / 1414
页数:12
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