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Bacterial Glycolipid Acting on Protein Transport Across Membranes.
Mori, Shoko; Shionyu, Masafumi; Shimamoto, Keiko; Nomura, Kaoru.
Affiliation
  • Mori S; Bioorganic Research Institute, Suntory Foundation for Life Sciences, 8-1-1 Seikadai, Seika-cho, Soraku-gun, Kyoto, 619-0284, Japan.
  • Shionyu M; Department of Frontier Bioscience, Nagahama Institute of Bio-Science and Technology, 1266 Tamura-cho, Nagahama, Shiga, 526-0829, Japan.
  • Shimamoto K; Bioorganic Research Institute, Suntory Foundation for Life Sciences, 8-1-1 Seikadai, Seika-cho, Soraku-gun, Kyoto, 619-0284, Japan.
  • Nomura K; Department of Chemistry Graduate School of Science, Osaka University, 1-1 Machikaneyama, Toyonaka, Osaka, 560-0043, Japan.
Chembiochem ; 25(10): e202300808, 2024 May 17.
Article in En | MEDLINE | ID: mdl-38400776
ABSTRACT
The process of protein transport across membranes involves a variety of factors and has been extensively investigated. Traditionally, proteinaceous translocons and chaperones have been recognized as crucial factors in this process. However, recent studies have highlighted the significant roles played by lipids and a glycolipid present in biological membranes in membrane protein transport. Membrane lipids can influence transport efficiency by altering the physicochemical properties of membranes. Notably, our studies have revealed that diacylglycerol (DAG) attenuates mobility in the membrane core region, leading to a dramatic suppression of membrane protein integration. Conversely, a glycolipid in Escherichia coli inner membranes, named membrane protein integrase (MPIase), enhances integration not only through the alteration of membrane properties but also via direct interactions with membrane proteins. This review explores the mechanisms of membrane protein integration mediated by membrane lipids, specifically DAG, and MPIase. Our results, along with the employed physicochemical analysis methods such as fluorescence measurements, nuclear magnetic resonance, surface plasmon resonance, and docking simulation, are presented to elucidate these mechanisms.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glycolipids / Cell Membrane / Protein Transport / Escherichia coli Language: En Journal: Chembiochem Journal subject: BIOQUIMICA Year: 2024 Document type: Article Affiliation country: Japan Country of publication: Germany

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Glycolipids / Cell Membrane / Protein Transport / Escherichia coli Language: En Journal: Chembiochem Journal subject: BIOQUIMICA Year: 2024 Document type: Article Affiliation country: Japan Country of publication: Germany