The laboratory of Ulrich Hartl at the Max Planck Institute for Biochemistry in Martinsried, Germany, has identified an archaeal homolog of prefoldin that also functions as a molecular chaperone.
42.
It appears that cellular levels of the enzyme may be controlled by the molecular chaperone HSP90, which upon association with CYP2E1 allows for transport to the proteasome and subsequent degradation.
43.
Because of the activity of polyphosphate as a molecular chaperone, strains of " E . coli " which accumulate polyphosphate could be used to increase yield of soluble recombinant protein.
44.
They act as molecular chaperones although they do not renature proteins and release them in the fashion of a true chaperone; instead, they bind improperly folded proteins to prevent protein aggregation.
45.
The stress proteins that are the main component of stress granules in plant cells are molecular chaperones that sequester, protect, and possibly repair proteins that unfold during heat and other types of stress.
46.
Beginning in the mid-1960s, investigators recognized that many HSPs function as molecular chaperones and thus play a critical role in protein folding, intracellular trafficking of proteins, and coping with proteins denatured by heat and other stresses.
47.
The regulation of transcription factors, effector proteins, molecular chaperones, and cytoskeletal proteins by acetylation and deacetylation is a significant post-translational regulatory mechanism These regulatory mechanisms are analogous to phosphorylation and dephosphorylation by the action of kinases and phosphatases.
48.
Polyphosphate accumulation is also of interest for a variety of industrial applications including removal of P i from aquatic environments via enhanced biological phosphorus removal and for its role as a molecular chaperone in expression of recombinant protein.
49.
So since the molecular chaperones are overexpressed in a wide variety of cancer cells and in virally transformed cells, inhibiting the function of these chaperones is essential to controlling cancer cells, as this would affect the activity of signaling proteins.
50.
The molecular chaperone BiP / Grp78 has a range of functions within the ER . It maintains specific transmembrane receptor proteins involved in initiating of the downstream signalling of the UPR in an inactive state by binding to their luminal domains.
