Gly-345 plays an essential role in Pyrococcus furiosus chaperonin function.
Biotechnol Lett
; 33(8): 1649-55, 2011 Aug.
Article
en En
| MEDLINE
| ID: mdl-21476092
ABSTRACT
Compared to the group I chaperonins, such as Escherichia coli GroEL, which facilitate protein folding, many aspects of the functional mechanism of archaeal group II chaperonins are unclear. Sequence homology between the chaperonin from Pyrococcus furiosus (PfCPN) and other group II chaperonins, together with the homo-oligomeric nature of PfCPN, suggest that PfCPN may serve as a model to clarify the role of the homologous position Gly-345 in the chaperonin-mediated protein folding. Here, we show that the purified chaperonin mutant in which the conserved residue Gly-345 is replaced by Asp (G345D) displays only about 25% ATP/ADP hydrolysis activities of the wild-type in the presence of Co(2+) and has a reduced capacity to promote folding of denatured malate dehydrogenase in vitro. This may be a reflection that Gly-345 plays an essential role in conformational change and protein refolding by archaeal group II chaperonins.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Proteínas Arqueales
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Pyrococcus furiosus
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Chaperoninas del Grupo II
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Glicina
Idioma:
En
Revista:
Biotechnol Lett
Año:
2011
Tipo del documento:
Article
País de afiliación:
China