Chaperone code: Difference between revisions

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{{coi|date=March 2013}}
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The ‘‘chaperone'''Chaperone code’’code''' has been identified as one of the main regulatory mechanism underlying cell function in biology. While the genetic code specifies how DNA makes proteins, while the histone code rules genomic transactions, the chaperone code stipulates how proteins produce a functional proteome.
The chaperone code refers to the combinatorial array of posttranslational modifications - i.e. phosphorylation, acetylation, ubiquitination, methylation, etc - that target molecular chaperones to modulate their activity. Molecular chaperones are proteins specialized in folding and unfolding of the other cellular proteins and assembly and dismantling of protein complexes, thereby orchestrating the dynamic organization of the proteome. As a consequence, a limited number of chaperones must be able to act on a very large number of substrates in a highly regulated manner.