We found a match
Your institution may have rights to this item. Sign in to continue.
- Title
Structural Requirements of a Glycolipid MPIase for Membrane Protein Integration.
- Authors
Fujikawa, Kohki; Han, Youjung; Osawa, Tsukiho; Mori, Shoko; Nomura, Kaoru; Muramoto, Maki; Nishiyama, Ken‐ichi; Shimamoto, Keiko
- Abstract
MPIase is a glycolipid involved in membrane protein integration in the inner membrane of Escherichia coli. To overcome the trace amounts and heterogeneity of natural MPIase, we systematically synthesized MPIase analogs. Structure‐activity relationship studies revealed the contribution of distinctive functional groups and the effect of the MPIase glycan length on membrane protein integration activity. In addition, both the synergistic effects of these analogs with the membrane chaperone/insertase YidC, and the chaperone‐like activity of the phosphorylated glycan were observed. These results verified the translocon‐independent membrane integration mechanism in the inner membrane of E. coli, in which MPIase captures the highly hydrophobic nascent proteins via its characteristic functional groups, prevents protein aggregation, attracts the proteins to the membrane surface, and delivers them to YidC in order to regenerate its own integration activity.
- Subjects
MEMBRANE proteins; GLYCOLIPIDS; ESCHERICHIA coli; STRUCTURE-activity relationships; FUNCTIONAL groups
- Publication
Chemistry - A European Journal, 2023, Vol 29, Issue 30, p1
- ISSN
0947-6539
- Publication type
Article
- DOI
10.1002/chem.202300437