About our group
The research in Strisovsky lab is focused on biological membranes and enzymatic catalysis occurring in their context. We are studying the ubiquitous intramembrane proteases of the rhomboid family and the mechanistic aspects of their functions relevant for biological signaling, membrane protein biogenesis and homeostasis. In our work we integrate the tools of membrane biochemistry, enzymology and structural biology to understand how rhomboid proteases recognise and select substrates, and employ methods of quantitative proteomics, cell biology and genetics to uncover molecular basis of rhomboid functions in organisms. We are an international group and we are always eager to consider motivated students and postdocs who would like to join us. If interested, contact Kvido Strisovsky.
1 February 2021
Hanka joins the group
Mgr. Hana Dvořáková joins the group. Welcome, Hanka! Looking forward to working with you.
3 January 2021
Blanka leaves the group.
Blanka Collis leaves the group after four great years as a postdoc. Many thanks for being with us and all the best in your new position!
1 October 2020
Jan Skerle passes his PhD viva!
Just before the autumnal season of coronavirus-induced limitations, Jan Skerle passes his PhD viva. Congratulations!
Rhomboid intramembrane protease YqgP licenses bacterial membrane protein quality control as adaptor of FtsH AAA protease
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…
The Rhomboid Superfamily: Structural Mechanisms and Chemical Biology Opportunities
Trends in Biochemical Sciences 43 (9): 726-739 (2018)
General and Modular Strategy for Designing Potent, Selective, and Pharmacologically Compliant Inhibitors of Rhomboid Proteases
Cell Chemical Biology 24 (12): 1523-1536 (2017)
Quantitative proteomics screen identifies a substrate repertoire of rhomboid protease RHBDL2 in human cells and implicates it in epithelial homeostasis
Scientific Reports 7: 7283 (2017)
Substrate binding and specificity of rhomboid intramembrane protease revealed by substrate-peptide complex structures
EMBO Journal 33 (20): 2408-2421 (2014)
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