Number of the records: 1  

Activity-Based Protein Profiling of Rhomboid Proteases in Liposomes

  1. 1.
    SYSNO ASEP0446560
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleActivity-Based Protein Profiling of Rhomboid Proteases in Liposomes
    Author(s) Wolf, E. V. (DE)
    Seybold, M. (DE)
    Hadravová, Romana (UOCHB-X) RID, ORCID
    Stříšovský, Kvido (UOCHB-X) RID, ORCID
    Verhelst, S. H. L. (DE)
    Number of authors5
    Source TitleChembiochem. - : Wiley - ISSN 1439-4227
    Roč. 16, č. 11 (2015), s. 1616-1621
    Number of pages6 s.
    Languageeng - English
    CountryDE - Germany
    Keywordsactivity-based protein profiling ; chemical probes ; inhibitors ; intramembrane proteases ; liposomes
    Subject RIVCE - Biochemistry
    R&D ProjectsLK11206 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    LO1302 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
    Institutional supportUOCHB-X - RVO:61388963
    UT WOS000358330300012
    EID SCOPUS84937251917
    DOI10.1002/cbic.201500213
    AnnotationAlthough activity-based protein profiling (ABPP) has been used to study a variety of enzyme classes, its application to intramembrane proteases is still in its infancy. Intramembrane proteolysis is an important biochemical mechanism for activating proteins residing within the membrane in a dormant state. Rhomboid proteases (intramembrane serine proteases) are embedded in the lipid bilayers of membranes and occur in all phylogenetic domains. The study of purified rhomboid proteases has mainly been performed in detergent micelle environments. Here we report on the reconstitution of rhomboids in liposomes. Using ABPP, we have been able to detect active rhomboids in large and giant unilamellar vesicles. We have found that the inhibitor profiles of rhomboids in micelles and liposomes are similar, thus validating previous inhibitor screenings. Moreover, fluorescence microscopy experiments on the liposomes constitute the first steps towards activity-based imaging of rhomboid proteases in membrane environments.
    WorkplaceInstitute of Organic Chemistry and Biochemistry
    Contactasep@uochb.cas.cz ; Kateřina Šperková, Tel.: 232 002 584 ; Viktorie Chládková, Tel.: 232 002 434
    Year of Publishing2016
Number of the records: 1  

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