CS
Kvido Stříšovský, PhD

Kvido Stříšovský, PhD

mail kvido.strisovskyinvalid-email-name@invalid-email-domainuochb.cas.cz
phone +420 220 183 468
Group leader
Kvido Stříšovský Group
Intramembrane Proteolysis and Biological Regulation
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Selected papers

Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease
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 J. Couté A. Galinier V. Veverka T. Doan K. Stříšovský
EMBO Journal 39 (10): e102935 (2020)
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…
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The Rhomboid Superfamily: Structural Mechanisms and Chemical Biology Opportunities
A. Tichá B. Collis K. Stříšovský
Trends in Biochemical Sciences 43 (9): 726-739 (2018)
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General and Modular Strategy for Designing Potent, Selective, and Pharmacologically Compliant Inhibitors of Rhomboid Proteases
A. Tichá S. Stanchev K. R. Vinothkumar D. C. Mikles P. Pachl J. Began J. Škerle K. Švehlová M. T. N. Nguyen S. H. L. Verhelst D. C. Johnson D. A. Bachovchin M. Lepšík P. Majer K. Stříšovský
Cell Chemical Biology 24 (12): 1523-1536 (2017)
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Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures
S. Zoll S. Stanchev J. Began J. Škerle M. Lepšík L. Peclinovská P. Majer K. Stříšovský
EMBO Journal 33 (20): 2408-2421 (2014)
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All publications

Latest publications

Extensive targeting of chemical space at the prime side of ketoamide inhibitors of rhomboid proteases by branched substituents empowers their selectivity and potency
K. Bach J. Dohnálek J. Škerlová J. Kuzmík E. Poláchová S. Stanchev P. Majer J. Fanfrlík A. Pecina J. Řezáč M. Lepšík V. Borshchevskiy V. Polovinkin K. Stříšovský
European Journal of Medicinal Chemistry 275: 116606 (2024)
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The Analysis of In-Membrane Nanoscopic Aggregation of Lipids and Proteins by MC-FRET
B. Chmelová J. Humpolíčková K. Stříšovský R. Šachl
Fluorescence Spectroscopy and Microscopy in Biology, Springer Series on Fluorescence Vol. 20 (R. Šachl & M. Amaro, Eds.), 1–26, Springer (2023)
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On the track of intramembrane clippers: the SPPL2a/b proteases caught in the act in animal models
K. Trávníčková K. Stříšovský
FEBS Journal 290 (9): 2306–2310 (2023)
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