Adaptor protein mediates dynamic pump assembly for bacterial metal efflux
Abstract
Multicomponent efflux pumps confer clinically relevant drug resistance in Gram-negative bacteria. These pumps, once assembled to function, traverse the periplasm linking inner and outer membranes tightly. However, little is known on how these pumps can operate efficiently without compromising periplasmic plasticity. We show here that in Escherichia coli , the tripartite complex CusCBA for Cu + and Ag + efflux exists as a dynamic structure and shifts toward the assembled form in response to metal stress. Unexpectedly, the periplasmic adaptor protein CusB is a key metal-sensing protein that mediates the complex assembly. This adaptor protein-mediated dynamic pump assembly allows the bacterial cell for efficient efflux on cellular demand while still maintaining periplasmic plasticity; it can be broadly relevant to other multicomponent efflux systems.
Document Details
- Document Type
- Pub Defense Publication
- Publication Date
- Jun 12, 2017
- Source ID
- 10.1073/pnas.1704729114
Entities
People
- Ace George Santiago
- Alayna M. George Thompson
- Lauren A Genova
- Megan M. Mcevoy
- Peng Chen
- Tai-Yen Chen
- Won Jung
Organizations
- Army Research Office
- Cornell University
- National Institute of Allergy and Infectious Diseases
- National Institute of General Medical Sciences
- University of Arizona
- University of California
- University of Houston