Editing GroEL (section)

{{Short description|Protein-coding gene in the species Homo sapiens}}
{{Infobox_gene}}
{{about|the bacterial and human mitochondrial gene|the protein family|HSP60}}
{{missing information|action in bacteria and chloroplasts|date=December 2020}}
'''GroEL''' is a protein which belongs to the [[chaperonin]] family of [[Chaperone (protein)|molecular chaperones]], and is found in many bacteria.<ref name="Zeilstra-Ryalls">{{cite journal | vauthors = Zeilstra-Ryalls J, Fayet O, Georgopoulos C | title = The universally conserved GroE (Hsp60) chaperonins | journal = Annu. Rev. Microbiol. | volume = 45 | pages = 301–25 | year = 1991 | pmid = 1683763 | doi = 10.1146/annurev.mi.45.100191.001505 }}</ref> It is required for the proper [[protein folding|folding]] of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex [[GroES]]. In [[eukaryotes]] the [[Organelle|organellar]] proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively, due to their endosymbiotic origin.

HSP60 is implicated in mitochondrial protein import and macromolecular assembly. It may facilitate the correct folding of imported proteins, and may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSP60 interacts with HRAS and with HBV protein X and HTLV-1 protein p40tax. HSP60 belongs to the chaperonin (HSP60) family. Note: This description may include information from UniProtKB.

Alternate Names: 	60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1

Heat shock protein 60 (HSP60) is a [[mitochondria]]l [[chaperonin]] that is typically held responsible for the transportation and refolding of proteins from the [[cytoplasm]] into the [[mitochondrial matrix]]. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear [[amino acid]] chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60’s [[bacterial]] homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Further studies have linked HSP60 to [[diabetes]], [[Stress (medicine)|stress]] response, [[cancer]] and certain types of [[immunological]] disorders.