Structure, function and regulation of the conserved serine proteases DegP and DegS of Escherichia coli.
Two members of the widely conserved HtrA family of serine proteases, DegP and DegS, are key players in extracytoplasmic protein quality control. The underlying mechanisms of their main functions in stress sensing, regulation and protection during the unfolded protein response are discussed.
Meltzer
Michael
M
Centre for Medical Biotechnology, FB Biology and Geography, University Duisburg-Essen, Unistr. 2, 45117 Essen, Germany.
Hasenbein
Sonja
S
Mamant
Nicolette
N
Merdanovic
Melisa
M
Poepsel
Simon
S
Hauske
Patrick
P
Kaiser
Markus
M
Huber
Robert
R
Krojer
Tobias
T
Clausen
Tim
T
Ehrmann
Michael
M
D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000378:metabolism*; D033903:Periplasmic Proteins / Q000737:chemistry* / Q000378:metabolism*; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000378:metabolism*
D029968:Escherichia coli Proteins; D006360:Heat-Shock Proteins; D033903:Periplasmic Proteins; C489349:degS protein, Escherichia coli; C061682:DegP protease; D012697:Serine Endopeptidases