![]() Taken together, these results show that the formation of HMW complexes is important for determining the RNA chaperone and protein chaperone activity of AtGRP4 and AtGRP7. Importantly, the additional 25 amino acids at the N-terminus of AtGRP4 are crucial for HMW complex formation and protein chaperone activity. Size exclusion chromatography and electron microscopy analyses revealed that the formation of high molecular weight (HMW) complexes is closely related to the protein chaperone activity of AtGRP4. The heat-induced thermal aggregation of a substrate protein was significantly decreased with the addition of AtGRP4 depending on protein concentration, whereas the thermal aggregation of a substrate protein was further increased with the addition of AtGRP7, demonstrating that AtGRP4 but not AtGRP7 possesses protein chaperone activity. Recent structural studies on these membrane chaperones have revealed their overall architecture, multi-subunit assembly, putative substrate transmembrane helix-binding pockets. The underlying functional principles of the different chaperone classes are beginning to be understood. They share the ability to recognize and bind nonnative proteins thus preventing unspecific aggregation. Here, two glycine-rich RNA-binding proteins in Arabidopsis thaliana (AtGRPs), AtGRP7 exhibiting RNA chaperone activity and AtGRP4 exhibiting no RNA chaperone activity, were investigated for their protein chaperone activity. Three such membrane chaperones have been described in the literaturethe endoplasmic reticulum membrane protein complex (EMC), the TMCO1 complex, and the PAT complex. The chaperone works to prevent folding defects and is a key player in the final steps of protein synthesis. Chaperones are a functionally related group of proteins assisting protein folding in the cell under physiological and stress conditions. Although many proteins possessing RNA chaperone or protein chaperone activity have been demonstrated in diverse organisms, report evaluating the RNA chaperone and protein chaperone activity of a given protein is severely limited. In molecular biology, molecular chaperones are proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular. Chaperone proteins as ameliorators of -synuclein-induced synaptic pathologies. RNA chaperones and protein chaperones are cellular proteins that can aid the correct folding of target RNAs and proteins, respectively.
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