CusC Heavy Metal Efflux Channel ofEscherichia Coli

Author(s):  
Jared A Delmar ◽  
Chih-Chia Su ◽  
Edward W Yu
Nature ◽  
2011 ◽  
Vol 470 (7335) ◽  
pp. 558-562 ◽  
Author(s):  
Chih-Chia Su ◽  
Feng Long ◽  
Michael T. Zimmermann ◽  
Kanagalaghatta R. Rajashankar ◽  
Robert L. Jernigan ◽  
...  

PLoS ONE ◽  
2011 ◽  
Vol 6 (1) ◽  
pp. e15610 ◽  
Author(s):  
Rithika Kulathila ◽  
Ragini Kulathila ◽  
Mridhu Indic ◽  
Bert van den Berg

2010 ◽  
Vol 76 (18) ◽  
pp. 6069-6076 ◽  
Author(s):  
Aurelio Moraleda-Muñoz ◽  
Juana Pérez ◽  
Antonio Luis Extremera ◽  
José Muñoz-Dorado

ABSTRACT Myxococcus xanthus has to cope with changes in its environment during growth and development. Among these factors, the concentration of copper is crucial due to the essential toxic effect of this metal, which forces the cells to maintain a tight homeostasis. The M. xanthus copper response is more complex than that in other bacteria, which is reflected by the different copper sensitivities of growing and developing cells. In the present study, the participation in copper homeostasis of six heavy metal efflux systems encoded in the M. xanthus genome has been examined. Three of these pumps exhibit the signature sequences in transmembrane domain 4 of the Cus systems (Cus1, Cus2, and Cus3), while the other three exhibit the motifs of the Czc systems (Czc1, Czc2, and Czc3). The Cus2 and Cus3 systems are inducible by copper and monovalent metals, functioning as the main copper efflux pumps, while the Cus1 system is implicated in Zn2+ homeostasis. The Czc systems are also differentially regulated either by divalent metals but not by copper (Czc1), by copper and divalent metals (Czc2), or by starvation (Czc3). The differential regulation of these six efflux systems ensures the proper completion of the M. xanthus life cycle in an environment with fluctuating concentrations of copper and other metals.


2013 ◽  
Vol 13 (1) ◽  
pp. 79 ◽  
Author(s):  
Estela Y Valencia ◽  
Vânia S Braz ◽  
Cristiane Guzzo ◽  
Marilis V Marques

mBio ◽  
2021 ◽  
Vol 12 (2) ◽  
Author(s):  
Mitchell A. Moseng ◽  
Meinan Lyu ◽  
Tanadet Pipatpolkai ◽  
Przemyslaw Glaza ◽  
Corey C. Emerson ◽  
...  

ABSTRACT Gram-negative bacteria utilize the resistance-nodulation-cell division (RND) superfamily of efflux pumps to expel a variety of toxic compounds from the cell. The Escherichia coli CusA membrane protein, which recognizes and extrudes biocidal Cu(I) and Ag(I) ions, belongs to the heavy-metal efflux (HME) subfamily of RND efflux pumps. We here report four structures of the trimeric CusA heavy-metal efflux pump in the presence of Cu(I) using single-particle cryo-electron microscopy (cryo-EM). We discover that different CusA protomers within the trimer are able to bind Cu(I) ions simultaneously. Our structural data combined with molecular dynamics (MD) simulations allow us to propose a mechanism for ion transport where each CusA protomer functions independently within the trimer. IMPORTANCE The bacterial RND superfamily of efflux pumps mediate resistance to a variety of biocides, including Cu(I) and Ag(I) ions. Here we report four cryo-EM structures of the trimeric CusA pump in the presence of Cu(I). Combined with MD simulations, our data indicate that each CusA protomer within the trimer recognizes and extrudes Cu(I) independently.


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