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Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion
Version 1
: Received: 25 December 2023 / Approved: 25 December 2023 / Online: 26 December 2023 (05:45:55 CET)
A peer-reviewed article of this Preprint also exists.
Nomura, K.; Mori, S.; Shimamoto, K. Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion. Membranes 2024, 14, 48. Nomura, K.; Mori, S.; Shimamoto, K. Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion. Membranes 2024, 14, 48.
Abstract
Membrane protein integrase (MPIase), an endogenous glycolipid in Escherichia coli (E. coli) membrane, is essential for membrane protein insertion in E. coli. We have examined Sec-independent membrane protein insertion mechanisms facilitated by MPIase using physicochemical analytical techniques such as solid-state nuclear magnetic resonance, fluorescence measurements, and surface plasmon resonance. In this review, we outline the physicochemical characteristics of membranes that may affect membrane insertion of proteins. Subsequently, we introduce our results verifying the effects of membrane lipids on insertion and estimate the impact of MPIase. Although MPIase is a minor component of E. coli membranes, it regulates insertion by altering the physicochemical properties of the membrane. In addition, MPIase promotes insertion by interacting with substrate proteins. We propose comprehensive mechanisms of membrane insertion of proteins involving MPIase, which provide a physicochemical basis for understanding the roles of glycolipids in protein translocation.
Keywords
glycolipids; Membrane protein; Sec-independent insertion; membrane lipids; physicochemical property of membrane
Subject
Biology and Life Sciences, Biophysics
Copyright: This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
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