Chaperones
Chaperones are group of proteins that oversee proper folding and the assembly of other macromolecular structures without being components of the final structure. This means these chaperones do not occur in these structures when the latter are performing their normal biological functions.chaperone function as the prevention or reversal of incorrect interactions that may occur when reactive macromolecular surfaces are transiently exposed to the intracellular environment
The term `molecular chaperone` was first used by Ron Laskey to describe the function of a particular protein useful for nucleosome formation and the term was later extended by John Ellis in 1987 to describe proteins that mediated the post-translational assembly of protein complexes.
Many people have a wrong perception that chaperones help only in proper folding of proteins but it is 100% correct as first chaperone to be discovered was nucleoplasmin which prevents the aggregation of folded histone proteins with DNA during the assembly of nucleosomes.Nucleoplasmin help in proper assembly of folded subunits into oligomeric structures and hence vital for DNA packaging.One major and more famous function of chaperones is to prevent both newly synthesised polypeptide chains and assembled subunits from aggregating into nonfunctional structures.Many chaperones are heat shock proteins but not all.These chaperones exists both in prokaryotes and eukaryotes.
References:
Lund PA.
The roles of molecular chaperones in vivo.
Essays Biochem. 1995;29:113-23
Hendrick JP, Hartl FU
The role of molecular chaperones in protein folding.
FASEB J. 1995 Dec;9(15):1559-69.
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