Recombinant Human GRPEL1 protein

GRPEL1 (GrpE-like 1) is a mitochondrial nucleotide exchange factor critical for maintaining protein homeostasis within the organelle. As a member of the GrpE family, it functionally interacts with mitochondrial heat shock protein 70 (mtHsp70), a chaperone central to protein import, folding, and quality control processes. GRPEL1 operates by regulating the ATPase cycle of mtHsp70. facilitating the release of ADP and promoting substrate protein binding during mitochondrial protein import and refolding of misfolded polypeptides.

Structurally, GRPEL1 contains conserved domains that enable its interaction with mtHsp70 and coordination of nucleotide exchange. Its localization to the mitochondrial matrix underscores its role in sustaining mitochondrial proteostasis, particularly under stress conditions. Studies have linked GRPEL1 deficiency to impaired mitochondrial function, including disrupted protein import machinery, accumulation of misfolded proteins, and increased susceptibility to oxidative stress. These dysfunctions are associated with neurodegenerative disorders such as Parkinson's disease, where mitochondrial impairment is a hallmark feature.

Recombinant GRPEL1 protein, typically produced using prokaryotic expression systems like E. coli, serves as a vital tool for mechanistic studies of mitochondrial chaperone networks. Its purified form enables in vitro analysis of Hsp70 interaction dynamics, nucleotide exchange rates, and chaperone-assisted protein folding pathways. Researchers also utilize recombinant GRPEL1 to model mitochondrial proteostasis in cellular systems and investigate its potential therapeutic relevance in diseases involving mitochondrial dysfunction. Recent evidence suggests GRPEL1 may influence metabolic adaptations in cancer cells, expanding its research significance beyond neurodegenerative contexts.