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Chaperones - Two Common Chaperone Systems: Hsp70 And Hsp60

proteins barrel polypeptide chains

Hsp70 chaperones (so called because their size is approximately 70,000 daltons, or atomic mass units) are a very large family of proteins whose amino acid sequences are very similar, indicating how important their structure is to their function. A single cell or cellular compartment may contain multiple Hsp70 chaperones, each with a specific function. In addition, the Hsp70 chaperones often work in concert with one or more smaller co-chaperone proteins, which serve to modulate the activity of the chaperone.

Some of the well-studied Hsp70 chaperones include DnaK from the bacterium Escherichia coli, the Ssa and Ssb proteins from yeast, and BiP (for "binding protein") from the mammalian endoplasmic reticulum. Hsp70 chaperones are often located where unfolded polypeptide chains typically appear. For example, Ssb chaperones associate with ribosomes, so that they are close to newly synthesized, unstructured polypeptide chains. It is thought that the binding of Hsp70 chaperones to these unfolded chains prevents inappropriate partial folding until the entire polypeptide chain is available for correct folding.

Hsp60 chaperones (also called "chaperonins") are barrel-shaped structures composed of fourteen to sixteen subunits of proteins that are approximately 60,000 daltons in size. Each subunit has a patch of non-polar amino acid groups lining the inner surface of the barrel; this patch recognizes the exposed non-polar amino acids of misfolded proteins. The binding and hydrolysis of ATP triggers conformational changes within the barrel, which (1) unfolds the misfolded conformation and releases the unfolded chain into the center of the barrel, (2) closes the top of the barrel with the binding of a co-chaperone "cap," and thereby (3) provides a protected environment in which correct folding can occur. Upon dissociation of the co-chaperone, the fully or partially folded protein is released into the general cellular environment.

The most extensively studied Hsp60 chaperones include GroEL from E. coli and TRiC/CCT from eukaryotic cells. GroEL appears to function as a general chaperone and interacts with 10 to 15 percent of all E. coli polypeptide chains, with a definite bias toward proteins that are small enough to fit within its central cavity. TRiC/CCT recognizes a much smaller set of proteins, and appears to play an additional role in the assembly of multiprotein complexes.

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