The HtrA family of proteases: implications for protein composition and cell fate.
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.
Clausen
Tim
T
Max-Planck-Institut für Biochemie, Abteilung Strukturforschung, Am Klopferspitz 18A, 82152 Martinsried, Germany.
Southan
Chris
C
Ehrmann
Michael
M
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism; D015195:Drug Design; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism; D008969:Molecular Sequence Data; D033903:Periplasmic Proteins / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D010802:Phylogeny; D017510:Protein Folding; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D012697:Serine Endopeptidases / Q000737:chemistry / Q000145:classification / Q000235:genetics / Q000378:metabolism*; D013696:Temperature
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D033903:Periplasmic Proteins; C061682:DegP protease; D012697:Serine Endopeptidases