Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus

Chen, Huayou; Tan, Xiao‐Li; Lü, Jian; Zhang, Chunxia; Zhang, Yi; Yang, Shengli

doi:10.1007/s10529-009-0070-x

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Cited by 2 publications

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References 15 publications

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“…To study the system in action under steady-state conditions, without accumulation of the competitive inhibitor ADP ( 27 ), we implemented an enzymatic system directly inside the NMR sample to ensure continuous rapid regeneration of ATP from ADP and phosphoenol pyruvate (PEP; Fig. 3A ).…”

Section: Resultsmentioning

confidence: 99%

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Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

et al. 2018

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Section: Resultsmentioning

confidence: 99%

“…3 and 4 , D and E, and figs. S9 and S10) ( 27 , 28 ). This view is corroborated by the absence of mixed conformations within a ring in EM images (fig.…”

Section: Discussionmentioning

confidence: 99%

Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

et al. 2018

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Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins

Hongo

Itai²,

Mizobata³

et al. 2011

The Journal of Biochemistry

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Prefoldin is a molecular chaperone found in the archaeal and eukaryotic cytosol. Prefoldin can stabilize tentatively nascent polypeptide chains or non-native forms of mainly cytoskeletal proteins, which are subsequently delivered to group II chaperonin to accomplish their precise folding. However, the detailed mechanism is not well known, especially with regard to endogenous substrate proteins. Here, we report the effects of Pyrococcus furiosus prefoldin (PfuPFD) on the refolding reactions of Pyrococcus furiosus citrate synthase (PfuCS) and Aequorea enhanced green fluorescence protein (GFPuv) in the presence or absence of Pyrococcus furiosus chaperonin (PfuCPN). We confirmed that both PfuPFD and PfuCPN interacted with PfuCS and GFPuv refolding intermediates. However, the interactions between chaperone and substrate were different for each case, as was the final effect on the refolding reaction. Effects on the refolding reaction varied from passive effects such as ATP-dependent binding and release (PfuCPN towards GFPuv) and binding which leads to folding arrest (PfuPFD towards GFPuv), to active effects such as net increase in thermal stability (PfuCPN towards PfuCS) to an active improvement in refolding yield (PfuPFD towards PfuCS). We postulate that differences in molecular interactions between substrate and chaperone lead to these differences in chaperoning effects.

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Characterization of ATPase activity of class II chaperonin from the hyperthermophilic archaeon Pyrococcus furiosus

Cited by 2 publications

References 15 publications

Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

Structural investigation of a chaperonin in action reveals how nucleotide binding regulates the functional cycle

Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins

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