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Characterization of the chaperone-like activity of HtrA (DegP) protein from Escherichia coli under the conditions of heat shock

✍ Scribed by Joanna Skorko-Glonek; Ewa Laskowska; Anna Sobiecka-Szkatula; Barbara Lipinska


Book ID
116177907
Publisher
Elsevier Science
Year
2007
Tongue
English
Weight
743 KB
Volume
464
Category
Article
ISSN
0003-9861

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The N-terminal region of HtrA heat shock
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HtrA heat shock protease is highly conserved in evolution, and in Escherichia coli, it protects the cell by degradation of proteins denatured by heat and oxidative stress, and also degrades misfolded proteins with reduced disulfide bonds. The mature, 48-kDa HtrA undergoes partial autocleavage with f