Wang, Lei; Bütikofer, Peter (2023). Lactose Permease Scrambles Phospholipids. Biology, 12(11) MDPI 10.3390/biology12111367
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Lactose permease (LacY) from Escherichia coli belongs to the major facilitator superfamily. It facilitates the co-transport of β-galactosides, including lactose, into cells by using a proton gradient towards the cell. We now show that LacY is capable of scrambling glycerophospholipids across a membrane. We found that purified LacY reconstituted into liposomes at various protein to lipid ratios catalyzed the rapid translocation of fluorescently labeled and radiolabeled glycerophospholipids across the proteoliposome membrane bilayer. The use of LacY mutant proteins unable to transport lactose revealed that glycerophospholipid scrambling was independent of H+/lactose transport activity. Unexpectedly, in a LacY double mutant locked into an occluded conformation glycerophospholipid, scrambling activity was largely inhibited. The corresponding single mutants revealed the importance of amino acids G46 and G262 for glycerophospholipid scrambling of LacY.
Item Type: |
Journal Article (Original Article) |
|---|---|
Division/Institute: |
04 Faculty of Medicine > Pre-clinic Human Medicine > Institute of Biochemistry and Molecular Medicine |
UniBE Contributor: |
Wang, Lei (B), Bütikofer, Peter |
Subjects: |
500 Science > 570 Life sciences; biology 600 Technology > 610 Medicine & health |
ISSN: |
2079-7737 |
Publisher: |
MDPI |
Language: |
English |
Submitter: |
Pubmed Import |
Date Deposited: |
28 Nov 2023 14:03 |
Last Modified: |
28 Nov 2023 14:13 |
Publisher DOI: |
10.3390/biology12111367 |
PubMed ID: |
37997967 |
Uncontrolled Keywords: |
LacY bilayer phospholipids scramblase symporter |
BORIS DOI: |
10.48350/189398 |
URI: |
https://boris.unibe.ch/id/eprint/189398 |
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