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Bulletin of the Korean Chemical Society (BKCS)

ISSN 0253-2964(Print)
ISSN 1229-5949(Online)
Volume 28, Number 12
BKCSDE 28(12)
December 20, 2007 

Nucleotide and Manganese Ion is Required for Chaperonin Function of
the Hyperthermostable Group II Chaperonin α from Aeropyrum pernix K1
Kyoung Jin Jang, Yu-Jin Bae, Sung-Jong Jeon, Kyunghwa Kim, Jung-Hee Lee, Sung Su Yea, Sangtaek Oh, Yong-Joo Jeong, Dong-Eun Kim*
Aeropyrum pernix, Archaea, Group II chaperonin, Nucleotide hydrolysis, Thermal aggregation
Prevention of thermal aggregation of the denatured protein by the group II chaperonin from the aerobic hyperthermophilic crenarchaeon Aeropyrum pernix K1 (ApcpnA) has been investigated. ApcpnA exists as a homo-oligomer in a ring structure, which protects thermal aggregation of the chemically denatured bovine rhodanese at 50 oC. ApcpnA alone is not sufficient for chaperonin activity, but the chaperonin activity is greatly enhanced in the presence of manganese ion and ATP. Compared to the mesophilic chaperonin GroEL/GroES, ApcpnA is more activated at a higher temperature and protects the aggregation-prone unfolded state of the denatured rhodanese from thermal aggregation. Binding of ATP is sufficient for ApcpnA to perform the chaperonin function in vitro, but hydrolysis of ATP is not necessarily required. We propose that utilization of Mn2+ and adenosine nucleotide regardless of ATP hydrolysis may be one of peculiar properties of archaeal chaperonins.
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