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Journal Article

The HtrA family of proteases: Implications for protein composition and cell fate

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons77864

Clausen,  T.
Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society;

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Clausen, T., Southan, C., & Ehrmann, M. (2002). The HtrA family of proteases: Implications for protein composition and cell fate. Molecular Cell, 10(3), 443-455.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6E62-1
Abstract
Cells precisely monitor the concentration and functionality of each protein for optimal performance. Protein quality control involves molecular chaperones, folding catalysts, and proteases that are often heat shock proteins. One quality control factor is HtrA, one of a new class of oligomeric serine proteases. The defining feature of the HtrA family is the combination of a catalytic domain with at least one C-terminal PDZ domain. Here, we discuss the properties and roles of this ATP-independent protease chaperone system in protein metabolism and cell fate.