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
✦ LIBER ✦
The Escherichia coli heat shock protease HtrA participates in defense against oxidative stress
✍ Scribed by Skórko-Glonek, J. ;Zurawa, D. ;Kuczwara, E. ;Wozniak, M. ;Wypych, Z. ;Lipinska, B.
- Publisher
- Springer
- Year
- 1999
- Tongue
- English
- Weight
- 301 KB
- Volume
- 262
- Category
- Article
- ISSN
- 0026-8925
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## Abstract High‐level expression of recombinant penicillin acylase (PAC) using the strong __trc__ promoter system in __Escherichia coli__ is frequently limited by the processing and folding of PAC precursors (proPAC) in the periplasm, resulting in physiological stress and inclusion body formation