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A cascading activity-based probe sequentially targets E1–E2–E3 ubiquitin enzymes

A cascading activity-based probe sequentially targets E1–E2–E3 ubiquitin enzymes

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Prüfsumme: MD5:723c04d1546e8d1d8618ce152de37b8c

MULDER, Monique P.C., Katharina WITTING, Ilana BERLIN, Jonathan N. PRUNEDA, Kuen-Phon WU, Jer-Gung CHANG, Johanna BIALAS, Marcus GROETTRUP, Farid EL OUALID, Huib OVAA, 2016. A cascading activity-based probe sequentially targets E1–E2–E3 ubiquitin enzymes. In: Nature Chemical Biology. 12(7), pp. 523-530. ISSN 1552-4450. eISSN 1552-4469

@article{Mulder2016-05-16casca-34794, title={A cascading activity-based probe sequentially targets E1–E2–E3 ubiquitin enzymes}, year={2016}, doi={10.1038/nchembio.2084}, number={7}, volume={12}, issn={1552-4450}, journal={Nature Chemical Biology}, pages={523--530}, author={Mulder, Monique P.C. and Witting, Katharina and Berlin, Ilana and Pruneda, Jonathan N. and Wu, Kuen-Phon and Chang, Jer-Gung and Bialas, Johanna and Groettrup, Marcus and El Oualid, Farid and Ovaa, Huib} }

<rdf:RDF xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:dcterms="http://purl.org/dc/terms/" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/rdf/resource/123456789/34794"> <dc:creator>Bialas, Johanna</dc:creator> <dc:contributor>Groettrup, Marcus</dc:contributor> <dc:contributor>Bialas, Johanna</dc:contributor> <dc:contributor>Pruneda, Jonathan N.</dc:contributor> <dc:language>eng</dc:language> <dc:contributor>Chang, Jer-Gung</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-07-15T09:58:57Z</dcterms:available> <dc:creator>Chang, Jer-Gung</dc:creator> <dcterms:title>A cascading activity-based probe sequentially targets E1–E2–E3 ubiquitin enzymes</dcterms:title> <dcterms:issued>2016-05-16</dcterms:issued> <dcterms:rights rdf:resource="http://nbn-resolving.de/urn:nbn:de:bsz:352-20150914100631302-4485392-8"/> <dc:creator>Witting, Katharina</dc:creator> <dc:contributor>Ovaa, Huib</dc:contributor> <dc:contributor>El Oualid, Farid</dc:contributor> <dc:contributor>Wu, Kuen-Phon</dc:contributor> <dc:creator>Groettrup, Marcus</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/34794"/> <dc:creator>Wu, Kuen-Phon</dc:creator> <dc:contributor>Berlin, Ilana</dc:contributor> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2016-07-15T09:58:57Z</dc:date> <dc:contributor>Mulder, Monique P.C.</dc:contributor> <dc:creator>El Oualid, Farid</dc:creator> <dcterms:abstract xml:lang="eng">Post-translational modifications of proteins with ubiquitin (Ub) and ubiquitin-like modifiers (Ubls), orchestrated by a cascade of specialized E1, E2 and E3 enzymes, control a wide range of cellular processes. To monitor catalysis along these complex reaction pathways, we developed a cascading activity-based probe, UbDha. Similarly to the native Ub, upon ATP-dependent activation by the E1, UbDha can travel downstream to the E2 (and subsequently E3) enzymes through sequential trans-thioesterifications. Unlike the native Ub, at each step along the cascade, UbDha has the option to react irreversibly with active site cysteine residues of target enzymes, thus enabling their detection. We show that our cascading probe 'hops' and 'traps' catalytically active Ub-modifying enzymes (but not their substrates) by a mechanism diversifiable to Ubls. Our founder methodology, amenable to structural studies, proteome-wide profiling and monitoring of enzymatic activity in living cells, presents novel and versatile tools to interrogate Ub and Ubl cascades.</dcterms:abstract> <dc:creator>Pruneda, Jonathan N.</dc:creator> <dc:creator>Ovaa, Huib</dc:creator> <dc:creator>Berlin, Ilana</dc:creator> <dc:contributor>Witting, Katharina</dc:contributor> <dc:creator>Mulder, Monique P.C.</dc:creator> </rdf:Description> </rdf:RDF>

Dateiabrufe seit 15.07.2016 (Informationen über die Zugriffsstatistik)

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