| Literature DB >> 21651889 |
Nacera Infed1, Nils Hanekop, Arnold J M Driessen, Sander H J Smits, Lutz Schmitt.
Abstract
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.Entities:
Mesh:
Substances:
Year: 2011 PMID: 21651889 DOI: 10.1016/j.bbamem.2011.05.016
Source DB: PubMed Journal: Biochim Biophys Acta ISSN: 0006-3002