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Titel:

A Photocrosslinking Probe to Capture the Substrates of Caseinolytic Protease P

Dokumenttyp:
Zeitschriftenaufsatz
Autor(en):
Sieber, Stephan Axel; Gronauer, Thomas F.; Eck, Laura K.; Ludwig, Christina
Abstract:
Protein homeostasis in bacteria is regulated by proteases such as the tetradecameric caseinolytic protease P (ClpP). Although substrates of ClpP have been successfully deciphered in genetically engineered cells, methods which directly trap processed proteins within native cells remain elusive. Here, we introduce an in situ trapping strategy which utilizes trifunctional probes that bind to the active site serine of ClpP and capture adjacent substrates with an attached photocrosslinking moiety. Af...     »
Stichworte:
BayBioMS; Caseinolytic protease P (ClpP); chemical proteomics; chemical biology; substrate traps; targeted proteomics
Zeitschriftentitel:
Angewandte Chemie International Edition
Jahr:
2024
Volltext / DOI:
doi:10.1002/anie.202409220
Verlag / Institution:
Wiley
E-ISSN:
1433-78511521-3773
Publikationsdatum:
29.07.2024
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