Pyrococcus prefoldin stabilizes protein-folding intermediates and transfers them to chaperonins for correct folding.
A molecular chaperone prefoldin/GimC from the hyperthermophilic archaeum Pyrococcus horikoshii OT3 was characterized. Pyrococcus prefoldin protected porcine heart citrate synthase from thermal aggregation whereas each subunit alone afforded little protection. It also arrested the spontaneous refolding of acid-denatured green fluorescent protein and then transferred it not only to a group II chaperonin from the hyperthermophilic archaeum Thermococcus sp. strain KS-1, but also to a group I chaperonin from the thermophilic bacterium Thermus thermophilus HB8 for subsequent ATP dependent refolding.
Okochi
Mina
M
Department of Biotechnology and Life Science, Tokyo University of Agriculture and Technology, 2-24-16, Naka-cho, Koganei, Tokyo 184-8588, Japan.
Yoshida
Takao
T
Maruyama
Tadashi
T
Kawarabayasi
Yutaka
Y
Kikuchi
Hisashi
H
Yohda
Masafumi
M
D000818:Animals; D018833:Chaperonins / Q000378:metabolism*; D002950:Citrate (si)-Synthase / Q000737:chemistry; D049452:Green Fluorescent Proteins; D006358:Hot Temperature; D007700:Kinetics; D008164:Luminescent Proteins / Q000737:chemistry; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D011489:Protein Denaturation; D017510:Protein Folding; D019711:Pyrococcus; D011994:Recombinant Proteins / Q000302:isolation & purification / Q000378:metabolism; D013552:Swine
D008164:Luminescent Proteins; D018832:Molecular Chaperones; D011994:Recombinant Proteins; C112806:prefoldin; D049452:Green Fluorescent Proteins; D002950:Citrate (si)-Synthase; D018833:Chaperonins