Journal
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
Volume 1808, Issue 9, Pages 2313-2321Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamem.2011.05.016
Keywords
Detergent screen; ABC transporter; Functional reconstitution; ATPase activity
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Funding
- Heinrich Heine University
- VW foundation [1/82 604]
- EU (EDICT (European Drug Initiative on Channels and Transporters)) [Health-2007-2.1.1.-5]
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The ABC transporter LmrA from Lactococcus lactis has been intensively studied and a role in multidrug resistance was proposed. Here, we performed a comprehensive detergent screen to analyze the impact of detergents for a successful solubilization, purification and retention of functional properties of this ABC transporter. Our screen revealed the preference of LmrA for zwitterionic detergents. In detergent solution, LmrA purified with FC-16 was highly active with respect to ATPase activity, which could be stimulated by a substrate (rhodamine 123) of LmrA Both, high ATPase activity and substrate stimulation were not detected for LmrA solubilized in DDM. Interestingly, reconstituted LmrA showed an opposite behavior, with a high basal ATPase activity and stimulation by rhodamine 123 for a DDM-reconstituted, but only low ATPase activity and no substrate stimulation for a FC-16 reconstituted sample. (C) 2011 Elsevier B.V. All rights reserved.
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