The mechanisms controlling membrane recognition by proteins with one hydrophobic stretch at their carboxyl terminus (tail anchor, TA) are poorly defined. The Escherichia coli TAs of ElaB and YqjD, which share sequential and structural similarity with the Saccharomyces cerevisiae TA of Fis1, were shown to localize to mitochondria. We show that YqjD and ElaB are directed by their TAs to bacterial cell poles. Fis1(TA) expressed in E. coli localizes like the endogenous TAs. The yeast and bacterial TAs are inserted in the E. coli inner membrane, and they all show affiliation to phosphatidic acid (PA), found in the membrane of the bacterial cell poles and of the yeast mitochondria. Our results suggest a mechanism for TA membrane recognition conserved from bacteria to mitochondria and raise the possibility that through their interaction with PA, and TAs play a role across prokaryotes and eukaryotes in controlling cell/organelle fate.
Bibliographical noteFunding Information:
We gratefully acknowledge Cory Dunn, whose enthusiasm, advice, and assistance throughout the experimental and writing stages made this work possible. We acknowledge Waldemar Vollmer, Sandy Parkinson, Victor Sourjik, Abram Aertsen, Thomas J. Silhavy, Cory Dunn, and Tom A. Rapoport for the gift of strains/plasmids/antibodies MHD63, RP437, NS89, IbpA‐msfGFP, NR754, HC575, HC962, HC342, b438‐442, and α‐SecY, respectively. We thank members of Orna Amster‐Choder lab for fruitful discussions and Yair Katz for help with western blots quantification. Research in OAC lab was supported by the Israel Science Foundation (ISF) founded by the Israel Academy of Sciences and Humanities (grant no. 1274/19).
© 2021 Federation of European Biochemical Societies
- bacterial cell poles
- evolutionary conservation
- membrane recognition
- phosphatidic acid
- protein localization
- tail-anchored proteins