Back

Prokaryotic phospholipid translocation by ubiquitous PplT domain proteins

Hauser, J. N.; Kengmo Tchoupa, A.; Zabel, S.; Nieselt, K.; Ernst, C. M.; Slavetinsky, C. J.; Peschel, A.

2022-03-12 microbiology
10.1101/2022.03.11.483950 bioRxiv
Show 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.

Matching journals

The top 9 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.