scholarly journals Assignment of the outer-membrane-subunit-selective domain of the membrane fusion protein in the tripartite xenobiotic efflux pump ofPseudomonas aeruginosa

2006 ◽  
Vol 254 (1) ◽  
pp. 101-107 ◽  
Author(s):  
Shima Eda ◽  
Hideaki Maseda ◽  
Eisaku Yoshihara ◽  
Taiji Nakae
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Outer Membrane ◽  
Efflux Pump ◽  
Membrane Fusion Protein

scholarly journals Substrate-Dependent Utilization of OprM or OpmH by the Pseudomonas aeruginosa MexJK Efflux Pump

2005 ◽  
Vol 49 (5) ◽  
pp. 2133-2136 ◽  
Author(s):  
Rungtip Chuanchuen ◽  
Takeshi Murata ◽  
Naomasa Gotoh ◽  
Herbert P. Schweizer
Keyword(s):  
Pseudomonas Aeruginosa ◽  
Cell Division ◽  
Membrane Proteins ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Outer Membrane ◽  
Protein Pair ◽  
Efflux Pump ◽  
Outer Membrane Proteins ◽  
Membrane Fusion Protein

ABSTRACT MexJK requires OprM for erythromycin efflux but not for triclosan efflux. Deletion of 15 OprM family outer membrane proteins (OMPs) revealed that only the TolC homolog OpmH functions with MexJK for triclosan efflux. This is the first report of natural utilization of multiple OMPs by a given resistance nodulation cell division transporter/membrane fusion protein pair.

scholarly journals Assembly and Channel Opening of Outer Membrane Protein in Tripartite Drug Efflux Pumps of Gram-negative Bacteria

2012 ◽  
Vol 287 (15) ◽  
pp. 11740-11750 ◽  
Author(s):  
Yongbin Xu ◽  
Arne Moeller ◽  
So-Young Jun ◽  
Minho Le ◽  
Bo-Young Yoon ◽  
...  
Keyword(s):  
Membrane Protein ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Outer Membrane ◽  
Outer Membrane Protein ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Membrane Fusion Protein ◽  
Docking Model ◽  
Channel Opening

Gram-negative bacteria are capable of expelling diverse xenobiotic substances from within the cell by use of three-component efflux pumps in which the energy-activated inner membrane transporter is connected to the outer membrane channel protein via the membrane fusion protein. In this work, we describe the crystal structure of the membrane fusion protein MexA from the Pseudomonas aeruginosa MexAB-OprM pump in the hexameric ring arrangement. Electron microscopy study on the chimeric complex of MexA and the outer membrane protein OprM reveals that MexA makes a tip-to-tip interaction with OprM, which suggests a docking model for MexA and OprM. This docking model agrees well with genetic results and depicts detailed interactions. Opening of the OprM channel is accompanied by the simultaneous exposure of a protein structure resembling a six-bladed cogwheel, which intermeshes with the complementary cogwheel structure in the MexA hexamer. Taken together, we suggest an assembly and channel opening model for the MexAB-OprM pump. This study provides a better understanding of multidrug resistance in Gram-negative bacteria.

scholarly journals Reviving Antibiotics: Efflux Pump Inhibitors That Interact with AcrA, a Membrane Fusion Protein of the AcrAB-TolC Multidrug Efflux Pump

2016 ◽  
Vol 3 (1) ◽  
pp. 89-98 ◽  
Author(s):  
Narges Abdali ◽  
Jerry M. Parks ◽  
Keith M. Haynes ◽  
Julie L. Chaney ◽  
Adam T. Green ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Membrane Fusion ◽  
Efflux Pump ◽  
Multidrug Efflux ◽  
Multidrug Efflux Pump ◽  
Membrane Fusion Protein ◽  
Efflux Pump Inhibitors

scholarly journals A membrane fusion protein, Ykt6, regulates epithelial cell migration via microRNA-mediated suppression of Junctional Adhesion Molecule A

Cell Cycle ◽  
2018 ◽  
Vol 17 (14) ◽  
pp. 1812-1831 ◽  
Author(s):  
Nayden G. Naydenov ◽  
Supriya Joshi ◽  
Alex Feygin ◽  
Siddharth Saini ◽  
Larisa Litovchick ◽  
...  
Keyword(s):  
Cell Migration ◽  
Epithelial Cell ◽  
Fusion Protein ◽  
Membrane Fusion ◽  
Adhesion Molecule ◽  
Membrane Fusion Protein ◽  
Epithelial Cell Migration
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