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Controlling the Activity of the 20S Proteasome Complex by Synthetic Gatekeepers
Author(s) -
Schulze Katrin,
Mulder Alart,
Tinazli Ali,
Tampé Robert
Publication year - 2006
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200600644
Subject(s) - proteasome , microbiology and biotechnology , chemistry , biochemistry , proteolysis , computational biology , biology , enzyme
Open sesame: The proteasome complex is a nanodegradation machine that is essential for cellular protein turnover. A multivalent chelator head (MCH) was exploited for the specific binding to histidine‐tagged proteasomes, even in crude cell lysates. Acting as synthetic gatekeepers, this MCH controls the access and thus the proteolytic activity of the nanomachinery.