지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
논문 기본 정보
- 자료유형
- 학술저널
- 저자정보
- 저널정보
- 한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology 제23권 제6호
- 발행연도
- 2013.1
- 수록면
- 818 - 825 (8page)
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초록· 키워드
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We isolated and functionally characterized the α- and β-subunits (ApCpnA and ApCpnB) of a chaperonin from Aeropyrum pernix K1. The constructed vectors pET3d-ApCpnA and pET21a-ApCpnB were transformed into E.
coli Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3)cells. The expression of ApCpnA (60.7 kDa) and ApCpnB (61.2 kDa) was confirmed by SDS-PAGE analysis.
Recombinant ApCpnA and ApCpnB were purified by heat-shock treatment and anion-exchange chromatography.
ApCpnA and ApCpnB were able to hydrolyze not only ATP, but also CTP, GTP, and UTP, albeit with different efficacies. Purified ApCpnA and ApCpnB showed the highest ATPase, CTPase, UTPase, and GTPase activities at 80oC. Furthermore, the addition of ApCpnA and ApCpnB effectively protected citrate synthase (CS) and alcohol dehydrogenase (ADH) from thermal aggregation and inactivation at 43oC and 50oC, respectively. In particular, the addition of ATP or CTP to ApCpnA and ApCpnB resulted in the most effective prevention of thermal aggregation and inactivation of CS and ADH.
The ATPase activity of the two chaperonin subunits was dependent on the salt concentration. Among the ions we examined, potassium ions were the most effective at enhancing the ATP hydrolysis activity of ApCpnA and ApCpnB.
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참고문헌 (25)
참고문헌 신청
Braig, K. / 1994 / The crystal structure of the bacterial chaperonin GroEL at 2.8 A / Nature 371 : 578 ~ 586
Buchner, J. / 1991 / GroE facilitates refolding of citrate synthase by suppressing aggregation / Biochemistry 30 : 1586 ~ 1591
Bukau, B. / 1998 / The Hsp70 and Hsp60 chaperone machines / Cell 92 : 351 ~ 366
Chang, Z. / 1996 / Mycobacterium tuberculosis 16-kDa antigen (Hsp 16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation / J. Biol. Chem 271 : 72
Chen, H. Y. / 2007 / Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus furiosus / J. Basic Microbiol 47 : 132
Buchner, J. / 1991 / GroE facilitates refolding of citrate synthase by suppressing aggregation / Biochemistry 30 : 1586 ~ 1591
Bukau, B. / 1998 / The Hsp70 and Hsp60 chaperone machines / Cell 92 : 351 ~ 366
Chang, Z. / 1996 / Mycobacterium tuberculosis 16-kDa antigen (Hsp 16.3) functions as an oligomeric structure in vitro to suppress thermal aggregation / J. Biol. Chem 271 : 72
Chen, H. Y. / 2007 / Expression and characterization of the chaperonin molecular machine from the hyperthermophilic archaeon Pyrococcus furiosus / J. Basic Microbiol 47 : 132
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