bioRxiv · 10.1101/2022.03.11.483950
Prokaryotic phospholipid translocation by ubiquitous PplT domain proteins
Abstract
Flippase proteins exchanging phospholipids between the cytoplasmic membrane leaflets have been identified in Eukaryotes but remained largely unknown in Prokaryotes. Only MprF proteins that synthesize aminoacyl phospholipids in some bacteria have been found to contain a domain that translocates the produced lipids. We show here that this domain, which we named prokaryotic phospholipid translocator (PplT), is widespread in Bacteria and Archaea, encoded as a separate protein or fused to different types of enzymes. We also demonstrate that the Escherichia coli PplT protein interacts with many phospholipid-synthetic enzymes and deletion of pplT impaired bacterial growth, which supports its potential role in membrane lipid metabolism. PplT domain proteins may be general prokaryotic lipid flippases with critical roles in cellular homeostasis.
Explore related subjects
Keep this discovery
Explore connections, maps & timelines
Hauser, J. N., Kengmo Tchoupa, A., Zabel, S., Nieselt, K., Ernst, C. M., Slavetinsky, C. J., Peschel, A.. 2022-03-12. Prokaryotic phospholipid translocation by ubiquitous PplT domain proteins. https://doi.org/10.1101/2022.03.11.483950
Cite the original work for its findings. Save a collection to share your selection of sources.