Cells precisely monitor the concentration and functionality of each protein for optimal
performance. Protein quality control involves molecular chaperones, folding catalysts, and …

Misfolding or unfolding of polypeptides can occur as a consequence of environmental stress
and spontaneous mutation. The abundance of general chaperones and proteases suggests …

We previously characterized a defective‐folding mutant of maltose‐binding protein of
Escherichia coli, MalE31, which formed periplasmic inclusion bodies. Here, we show that …

Enhancement of the production of soluble recombinant penicillin acylase in Escherichia coli
via coexpression of a periplasmic protease/chaperone, DegP, was demonstrated …

The high-temperature requirement A (HtrA) family of serine proteases has been shown to
play an important role in the environmental and cellular stress damage control system in …

DegP (HtrA) is a periplasmic heat shock serine protease of Escherichia coli that degrades
misfolded proteins at high temperatures. Biochemical and biophysical experiments have …

Ferric‐binding proteins (FbpA) have been implicated in the transferrin receptor‐mediated
iron acquisition pathways of Haemophilus influenzae and Neisseria spp. These proteins are …

Functional expression of recombinant Pseudozyma antarctica lipase B (PalB) in Escherichia
coli was explored. While PalB was stably expressed in the cytoplasm, most of the expressed …

Most biochemical, computational and genetic approaches to gene finding assume the
Central Dogma and look for genes that make mRNA and have ORFs. These approaches …

Escherichia coli DegP, also known as HtrA or protease Do, is a periplasmic serine protease
which is essential for the viability of the cell at elevated temperatures (Lipinska et al., 1990; …