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Allosteric Activation of HtrA Protease DegP by Stress Signals during Bacterial Protein Quality Control
Author(s) -
Meltzer Michael,
Hasenbein Sonja,
Hauske Patrick,
Kucz Nicolette,
Merdanovic Melisa,
Grau Sandra,
Beil Alexandra,
Jones Dafydd,
Krojer Tobias,
Clausen Tim,
Ehrmann Michael,
Kaiser Markus
Publication year - 2008
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.200703273
Subject(s) - allosteric regulation , protease , proteases , peptide , residue (chemistry) , biochemistry , chemistry , enzyme , microbiology and biotechnology , biology
Unleashing the proteolytic activity of DegP : A study with synthetic mimics of cellular stress signals reveals an allosteric (chemical) activation mechanism of the bacterial HtrA protease DegP, leading to a fine‐tuned amplification of protein degradation during bacterial protein quality control (see scheme: binding of a peptide sequence (circles) increases activation. The nature of the penultimate residue (red) is shown to be decisive).