Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion
Membrane protein integrase (MPIase), an endogenous glycolipid in <i>Escherichia coli</i> (<i>E. coli</i>) membranes, is essential for membrane protein insertion in <i>E. coli</i>. We have examined Sec-independent membrane protein insertion mechanisms facilitated b...
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| Format: | Article |
| Language: | English |
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MDPI AG
2024-02-01
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| Series: | Membranes |
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| Online Access: | https://www.mdpi.com/2077-0375/14/2/48 |
| _version_ | 1797297555306971136 |
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| author | Kaoru Nomura Shoko Mori Keiko Shimamoto |
| author_facet | Kaoru Nomura Shoko Mori Keiko Shimamoto |
| author_sort | Kaoru Nomura |
| collection | DOAJ |
| description | Membrane protein integrase (MPIase), an endogenous glycolipid in <i>Escherichia coli</i> (<i>E. coli</i>) membranes, is essential for membrane protein insertion in <i>E. coli</i>. We have examined Sec-independent membrane protein insertion mechanisms facilitated by MPIase using physicochemical analytical techniques, namely 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 <i>E. coli</i> 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 for the membrane insertion of proteins involving MPIase, which provide a physicochemical basis for understanding the roles of glycolipids in protein translocation. |
| first_indexed | 2024-03-07T22:21:59Z |
| format | Article |
| id | doaj.art-9c106aeb08034fe4b270f4a956b73e6f |
| institution | Directory Open Access Journal |
| issn | 2077-0375 |
| language | English |
| last_indexed | 2024-03-07T22:21:59Z |
| publishDate | 2024-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Membranes |
| spelling | doaj.art-9c106aeb08034fe4b270f4a956b73e6f2024-02-23T15:26:55ZengMDPI AGMembranes2077-03752024-02-011424810.3390/membranes14020048Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein InsertionKaoru Nomura0Shoko Mori1Keiko Shimamoto2Bioorganic Research Institute, Suntory Foundation for Life Sciences, 8-1-1 Seikadai, Seika-cho, Soraku-gun, Kyoto 619-0284, JapanBioorganic Research Institute, Suntory Foundation for Life Sciences, 8-1-1 Seikadai, Seika-cho, Soraku-gun, Kyoto 619-0284, JapanBioorganic Research Institute, Suntory Foundation for Life Sciences, 8-1-1 Seikadai, Seika-cho, Soraku-gun, Kyoto 619-0284, JapanMembrane protein integrase (MPIase), an endogenous glycolipid in <i>Escherichia coli</i> (<i>E. coli</i>) membranes, is essential for membrane protein insertion in <i>E. coli</i>. We have examined Sec-independent membrane protein insertion mechanisms facilitated by MPIase using physicochemical analytical techniques, namely 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 <i>E. coli</i> 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 for the membrane insertion of proteins involving MPIase, which provide a physicochemical basis for understanding the roles of glycolipids in protein translocation.https://www.mdpi.com/2077-0375/14/2/48glycolipidsmembrane proteinSec-independent insertionmembrane lipidsphysicochemical property of membrane |
| spellingShingle | Kaoru Nomura Shoko Mori Keiko Shimamoto Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion Membranes glycolipids membrane protein Sec-independent insertion membrane lipids physicochemical property of membrane |
| title | Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion |
| title_full | Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion |
| title_fullStr | Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion |
| title_full_unstemmed | Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion |
| title_short | Roles of a Glycolipid MPIase in Sec-Independent Membrane Protein Insertion |
| title_sort | roles of a glycolipid mpiase in sec independent membrane protein insertion |
| topic | glycolipids membrane protein Sec-independent insertion membrane lipids physicochemical property of membrane |
| url | https://www.mdpi.com/2077-0375/14/2/48 |
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