Functional Characterization of Recombinant Prefoldin Complexes from a Hyperthermophilic Archaeon, Thermococcus sp. Strain KS-1

Thermodynamic Characterization of the Interaction between Prefoldin and Group II Chaperonin

“…11,12 We have studied the mechanism of protein folding mediated by the archaeal PFD-CPN system. 9,10,13 PhPFD and PFDs of Thermococcus strain KS-1 (T. KS-1) can capture an acid-denatured green fluorescence protein (GFP) and transfer it to T. KS-1 CPN for ATPdependent folding. The release of a substrate protein from PhPFD is facilitated by T. KS-1 CPN.…”

“…KS-1 expresses two pairs of PFD subunits genes: two α-subunit genes pfdα 1 and pfdα 2 , and two β-subunit genes pfdβ 1 and pfdβ 2 . 13 We have functionally characterized four recombinant T. KS-1 PFD complexes (PFDα1-β1, PFDα1-β2, PFDα2-β1, and PFDα2-β2). 13 All four complexes make similar heterohexameric structures and exhibit chaperone activity to suppress thermal aggregation.…”

“…13 We have functionally characterized four recombinant T. KS-1 PFD complexes (PFDα1-β1, PFDα1-β2, PFDα2-β1, and PFDα2-β2). 13 All four complexes make similar heterohexameric structures and exhibit chaperone activity to suppress thermal aggregation. Moreover, the transfer of a denatured GFP to CPNα for folding was demonstrated for PFDα1-β1.…”

Cavity Control of Prefoldin Nano Actuator (PNA) by Temperature and pH

“…Each subunit has a hydrophobic groove at the distal region where an unfolded substrate protein is bound. Each tentacle belongs to one of the six Prefoldin subunits, arranged as two subunits (151 amino acids) located in the center of the structure and four of the homologous subunits (117 amino acids) placed at the periphery [21].…”

Co-expression of chaperones from P. furiosus enhanced the soluble expression of the recombinant hyperthermophilic α-amylase in E. coli

“…Archaeal prefoldin is a hexameric molecular chaperone complex containing two α-subunits and four β-subunits. Previous studies indicated that archaeal prefoldins were able to protect the aggregation of diverse heterogeneous proteins (Iizuka et al 2008;Leroux et al 1999;Laksanalamai et al 2006;Okochi et al 2002;Lundin et al 2004;Hongo et al 2012). Furthermore, overexpression of prefoldin from hyperthermophilic archaea was able to efficiently increase tolerance of E. coli hosts to different environmental stresses, such as the presence of an organic solvent (Okochi et al 2008) or high temperature (Chen et al 2010).…”