PMID: 3112578</ref> Besides, chaperones help in targeting the native proteins to their respective organelles [1][2] The first identified chaperones were the histone chaperones that are continously involved in histone metabolism thus regulating genome function, stability and identity[3]. Many protozoan parasites such as Plasmodium falciparum requires these proteins for cytoprotection [4] [5]Chaperones actively participate in the maintenance of proteome integrity, and protein homeostasis (proteostasis) which requires a syncrhonization in various chaperones tuning the process [6].
Disease
Chaperones are instrumental in protein folding processes. Any alteration in this process leads to protein aggregation and formation of inclusion bodies. Protein misfolding results in various diseases such as Alzheimer[7],Cytosolic neurofibrillatory tangles,Parkinson[8],Familial amyotrophic lateral sclerosis, Huntington, Spinocerebellar ataxia 1, 2, 3, disease, Spinobulbar muscular atrophy and ageing[9].
Relevance
Modulation of chaperones expression is the new therapeutic approach for neurodegenerative and other disease arising from protein misfolding. There is a distinct network of chaperones and co chaperones that either directly influences the substrate proteins or in association with the protein degradation pathways such as the ubiquitin-proteasome-system or autophagy, results in the removal of completely misfolded and pathogenic proteins[10].
Structural highlights
Structurally, heat shock proteins have a N-terminal followed by a with elongated C-terminal. is a representative example of a chaperone system in complex with ADP.
