Rhomboid-catalyzed intramembrane proteolysis requires hydrophobic matching with the surrounding lipid bilayer.

Autor:	Engberg O; Institute for Medical Physics and Biophysics, University of Leipzig, Härtelstr. 16/18, D-04107 Leipzig, Germany., Ulbricht D; Institute for Medical Physics and Biophysics, University of Leipzig, Härtelstr. 16/18, D-04107 Leipzig, Germany., Döbel V; Institute for Medical Physics and Biophysics, University of Leipzig, Härtelstr. 16/18, D-04107 Leipzig, Germany., Siebert V; Center for Molecular Biology of Heidelberg University (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany.; Center for Biochemistry and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Cologne, Germany., Frie C; Center for Biochemistry and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Cologne, Germany., Penk A; Institute for Medical Physics and Biophysics, University of Leipzig, Härtelstr. 16/18, D-04107 Leipzig, Germany., Lemberg MK; Center for Molecular Biology of Heidelberg University (ZMBH), Im Neuenheimer Feld 282, D-69120 Heidelberg, Germany.; Center for Biochemistry and Cologne Excellence Cluster on Cellular Stress Responses in Aging-Associated Diseases (CECAD), Medical Faculty, University of Cologne, Joseph-Stelzmann-Str. 52, D-50931 Cologne, Germany., Huster D; Institute for Medical Physics and Biophysics, University of Leipzig, Härtelstr. 16/18, D-04107 Leipzig, Germany.
Jazyk:	angličtina
Zdroj:	Science advances [Sci Adv] 2022 Sep 23; Vol. 8 (38), pp. eabq8303. Date of Electronic Publication: 2022 Sep 23.
DOI:	10.1126/sciadv.abq8303
Abstrakt:	Membrane thinning by rhomboid proteins has been proposed to reduce hydrophobic mismatch, providing a unique environment for important functions ranging from intramembrane proteolysis to retrotranslocation in protein degradation. We show by in vitro reconstitution and solid-state nuclear magnetic resonance that the lipid environment of the Escherichia coli rhomboid protease GlpG influences its activity with an optimal hydrophobic membrane thickness between 24 and 26 Å. While phosphatidylcholine membranes are only negligibly altered by GlpG, in an E. coli -relevant lipid mix of phosphatidylethanolamine and phosphatidylglycerol, a thinning by 1.1 Å per leaflet is observed. Protease activity is strongly correlated with membrane thickness and shows no lipid headgroup specificity. We infer from these results that, by adjusting the thickness of specific membrane domains, membrane proteins shape the bilayer for their specific needs.
Databáze:	MEDLINE
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