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Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease

J. Began, B. Cordier, J. Březinová, J. Delisle, R. Hexnerová, P. Srb, P. Rampírová, M. Kožíšek, M. Baudet, Y. Couté, A. Galinier, V. Veverka, T. Doan, K. Strisovsky,

. 2020 ; 39 (10) : e102935. [pub] 20200113

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc20028172

Grantová podpora
LO1302 Ministerstvo Školství, Mládeže a Tělovýchovy (MEYS) - International
CZ.02.1.01/0.0/0.0/16_019/0000729 EC European Regional Development Fund (ERDF) - International
ANR-10-INBS-08-01 Agence Nationale de la Recherche (ANR) - International
170214 GrantováAgentura, Univerzita Karlova (GA UK) - International
PIRG08-GA-2010-276750 EC FP7 FP7 Ideas: European Research Council (FP7 Ideas) - International
Gilead Sciences & IOCB Research Centre - International
61388963 National Subvention for Development of Research Organisations - International
CNRS - International
PIRG08-GA-2010-276750 Marie-Curie International Reintegration Grant - International
Aix-Marseille University (AMU) - International
FDT20160435133 Fondation pour la Recherche Médicale - International
18-09556S Czech Science Foundation - International

Magnesium homeostasis is essential for life and depends on magnesium transporters, whose activity and ion selectivity need to be tightly controlled. Rhomboid intramembrane proteases pervade the prokaryotic kingdom, but their functions are largely elusive. Using proteomics, we find that Bacillus subtilis rhomboid protease YqgP interacts with the membrane-bound ATP-dependent processive metalloprotease FtsH and cleaves MgtE, the major high-affinity magnesium transporter in B. subtilis. MgtE cleavage by YqgP is potentiated in conditions of low magnesium and high manganese or zinc, thereby protecting B. subtilis from Mn2+ /Zn2+ toxicity. The N-terminal cytosolic domain of YqgP binds Mn2+ and Zn2+ ions and facilitates MgtE cleavage. Independently of its intrinsic protease activity, YqgP acts as a substrate adaptor for FtsH, a function that is necessary for degradation of MgtE. YqgP thus unites protease and pseudoprotease function, hinting at the evolutionary origin of rhomboid pseudoproteases such as Derlins that are intimately involved in eukaryotic ER-associated degradation (ERAD). Conceptually, the YqgP-FtsH system we describe here is analogous to a primordial form of "ERAD" in bacteria and exemplifies an ancestral function of rhomboid-superfamily proteins.

Citace poskytuje Crossref.org

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$a Magnesium homeostasis is essential for life and depends on magnesium transporters, whose activity and ion selectivity need to be tightly controlled. Rhomboid intramembrane proteases pervade the prokaryotic kingdom, but their functions are largely elusive. Using proteomics, we find that Bacillus subtilis rhomboid protease YqgP interacts with the membrane-bound ATP-dependent processive metalloprotease FtsH and cleaves MgtE, the major high-affinity magnesium transporter in B. subtilis. MgtE cleavage by YqgP is potentiated in conditions of low magnesium and high manganese or zinc, thereby protecting B. subtilis from Mn2+ /Zn2+ toxicity. The N-terminal cytosolic domain of YqgP binds Mn2+ and Zn2+ ions and facilitates MgtE cleavage. Independently of its intrinsic protease activity, YqgP acts as a substrate adaptor for FtsH, a function that is necessary for degradation of MgtE. YqgP thus unites protease and pseudoprotease function, hinting at the evolutionary origin of rhomboid pseudoproteases such as Derlins that are intimately involved in eukaryotic ER-associated degradation (ERAD). Conceptually, the YqgP-FtsH system we describe here is analogous to a primordial form of "ERAD" in bacteria and exemplifies an ancestral function of rhomboid-superfamily proteins.
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