期刊
SCIENTIFIC REPORTS
卷 5, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/srep17037
关键词
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资金
- National Key Basic Research Program of China [2012CB518000]
- National Natural Science Foundation of China [21503278, 21033005, 21073236]
- China Postdoctoral Science Foundation [2015T80756, 2014M560588]
- Doctoral Foundation of Shandong Province [BS2013SW035]
- Project of Science and Technology Program for Basic Research of Qingdao [13-1-4-237-jch]
- Fundamental Research Funds for the Central Universities [R1404031A, R1304012A]
- Natural Science Foundation for Distinguished Young Scholars of Shandong Province [JQ201008]
The in vitro folding of newly translated human CC chemokine receptor type 5 (CCR5), which belongs to the physiologically important family of G protein-coupled receptors (GPCRs), has been studied in a cell-free system supplemented with the surfactant Brij-35. The freshly synthesized CCR5 can spontaneously fold into its biologically active state but only slowly and inefficiently. However, on addition of the GroEL-GroES molecular chaperone system, the folding of the nascent CCR5 was significantly enhanced, as was the structural stability and functional expression of the soluble form of CCR5. The chaperonin GroEL was partially effective on its own, but for maximum efficiency both the GroEL and its GroES lid were necessary. These results are direct evidence for chaperone-assisted membrane protein folding and therefore demonstrate that GroEL-GroES may be implicated in the folding of membrane proteins.
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