Chaperones: Difference between revisions

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Gauri Misra, Michal Harel, Alexander Berchansky

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 <StructureSection load='Heat shock proteins' size='340' side='right' caption='' scene='59/591341/Heat_shock_proteins/1'>
-Chaperones are proteins that are involved in the folding and unfolding of other macromolecules. The word chaperone means giving protection which implies the idea of preventing new proteins from misfolding. They exists both in prokaryotes and eukaryotes. Some chaperones are constitutively expressed in the system where as other chaperones are expressed only in response to an external stimulus or stress such as heat and therefore they are referred to as ''heat shock proteins''. They are classified based on their structure, size, molecular weight and function in to several classes such as [[Hsp40s]], Hsp60s [[Chaperonin]], Hsp70s, Hsp90s such as [[1am1]], [[Hsp100s]] and small heat shock proteins like (alpha)-crystallin proteins. Various classes of molecular chaperones cooperate for the folding of the nascent polypeptide chains in the cyotplasm <ref>doi: 10.1146/annurev-biochem-060208-092442</ref>.
+Chaperones are proteins that are involved in the folding and unfolding of other macromolecules. The word chaperone means 'giving protection' which implies the idea of preventing new proteins from misfolding. They exists both in prokaryotes and eukaryotes. Some chaperones are constitutively expressed in the system where as other chaperones are expressed only in response to an external stimulus or stress such as heat and therefore they are referred to as ''heat shock proteins''. They are classified based on their structure, size, molecular weight and function in to several classes such as [[Hsp40s]], Hsp60s [[Chaperonin]], Hsp70s, Hsp90s such as [[1am1]], [[Hsp100s]] and small heat shock proteins like (alpha)-crystallin proteins. Various classes of molecular chaperones cooperate for the folding of the nascent polypeptide chains in the cyotplasm <ref>doi: 10.1146/annurev-biochem-060208-092442</ref>.
 == Function ==
 Chaperones bind to the newly synthesized and unfolded proteins helping them acquire their properly folded 3D structure <ref>PMID: 3112578</ref>. Besides, chaperones help in targeting the native proteins to their respective organelles <ref>PMID:3282178</ref><ref>DOI: 10.1002/iub.1272</ref>. The first identified chaperones were the histone chaperones that are continously involved in histone metabolism thus regulating genome function, stability and identity<ref>doi: 10.1146/annurev-biochem-060713-035536</ref>. Many protozoan parasites such as ''Plasmodium falciparum'' requires these proteins for cytoprotection <ref>PMID: 14711509</ref> <ref>PMID: 19339102</ref>. Chaperones actively participate in the maintenance of proteome integrity and protein homeostasis (proteostasis) which requires a syncrhonization in various chaperone's tuning the process <ref>DOI: 10.1146/annurev-biochem-060208-092442</ref>.