Mitochondria import many hundreds of different proteins that are encoded by nuclear genes.
These proteins are targeted to the mitochondria, translocated through the mitochondrial …

The chaperone protein network controls both initial protein folding and subsequent
maintenance of proteins in the cell. Although the native structure of a protein is principally …

Escherichia coli FtsH is an essential integral membrane protein that has an AAA‐type
ATPase domain at its C‐terminal cytoplasmic part, which is homologous to at least three …

THE FUNCTION OF Hsp70 proteins as molecular chaperones in mediating the biogenesis
of proteins has been known for quite some time. The basic mechanism of action for these …

▪ Abstract Envelope stress responses play important pysiological roles in a variety of
processes, including protein folding, cell wall biosynthesis, and pathogenesis. Many of these …

Disruption of normal protein trafficking in the Escherichia coli cell envelope (inner
membrane, periplasm, outer membrane) can activate two parallel, but distinct, signal …

▪ Abstract A mechanism for regulating gene expression at the level of transcription utilizes an
antagonist of the sigma transcription factor known as the anti-sigma (anti-σ) factor. The …

The Escherichia coli Hsp40 DnaJ and Hsp70 DnaK cooperate in the binding of proteins at
intermediate stages of folding, assembly, and translocation across membranes. Binding of …

The Escherichia coli endoribonuclease RNase E is essential for RNA processing and
degradation. Earlier work provided evidence that RNase E exists intracellularly as part of a …

The extracytoplasmic stress response in Escherichia coli is controlled by the alternative
sigma factor, σE. σE activity is uniquely induced by the accumulation of outer membrane …