The HtrA Family of Proteases: Implications for Protein Composition and Cell Fate

• Published in: Molecular Cell Vol. 10; no. 3; pp. 443 - 455
• Main Authors: Clausen, Tim, Southan, Chris, Ehrmann, Michael
• Format: Book Review Journal Article
• Language: English
• Published: United States Elsevier Inc 01.09.2002
• Subjects: Amino Acid Sequence; Bacterial Proteins - chemistry; Bacterial Proteins - classification; Bacterial Proteins - genetics; Bacterial Proteins - metabolism; Drug Design; Gene Expression Regulation, Bacterial; Heat-Shock Proteins - chemistry; Heat-Shock Proteins - classification; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Humans; Models, Molecular; Molecular Chaperones - metabolism; Molecular Sequence Data; Periplasmic Proteins - chemistry; Periplasmic Proteins - classification; Periplasmic Proteins - genetics; Periplasmic Proteins - metabolism; Phylogeny; Protein Folding; Protein Structure, Tertiary; Sequence Alignment; Serine Endopeptidases - chemistry; Serine Endopeptidases - classification; Serine Endopeptidases - genetics; Serine Endopeptidases - metabolism; Temperature
• ISSN: 1097-2765; 1097-4164
• DOI: 10.1016/S1097-2765(02)00658-5

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.