Structural and Molecular Characterization of the Prefoldin β Subunit from Thermococcus Strain KS-1

Kida, Hiroshi; Sugano, Yuki; Iizuka, Ryo; Fujihashi, M.; Yohda, Masafumi; Miki, Kunio

doi:10.1016/j.jmb.2008.08.041

Cited by 25 publications

(17 citation statements)

References 34 publications

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“…This coiled-coil/substrate size dependence has been observed for other archaeal PFDs [24]. The archaeon Thermococcus kodakaraensis KOD1 possesses two sets of the PFD b subunit (b1 and b2).…”

Section: Docking Of Non-native Protein Substrates To Cpfd Filamentssupporting

confidence: 57%

“…It is probable that the shorter length capped filaments containing four cPFD subunits would be sufficient to protect against thermal aggregation of small substrates. This coiled-coil/substrate size dependence has been observed for other archaeal PFDs [24]. The archaeon Thermococcus kodakaraensis KOD1 possesses two sets of the PFD b subunit (b1 and b2).…”

Section: Determining the Minimal Length Of Cpfd Filaments For Chaperosupporting

confidence: 57%

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Oligomeric assembly is required for chaperone activity of the filamentous γ‐prefoldin

Glover

Clark

2015

The FEBS Journal

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Prefoldins (PFDs) are molecular chaperones with a distinctive jellyfishshape that have a general role in de novo protein folding in Archaea and in the biogenesis of cytoskeleton proteins in eukaryotes. In general, PFDs are hetero-hexameric protein assemblies consisting of two a and four b subunits. However, a PFD variant called gamma-prefoldin (cPFD), isolated from the hyperthermophilic archaeon Methanocaldococcus jannaschii, exhibits a unique filamentous structure that is composed of hundreds of monomeric subunits. In this study, we investigated the relationship between the morphology of the cPFD filament and its ability to prevent protein aggregation. A chaperone assay demonstrated that cPFD must be in a filamentous assembly for functional activity and the distal regions of the coiled-coils are required for binding of non-native proteins. Molecular dynamic simulations were used to model the interactions between in silico thermally denatured protein substrates and the coiled-coils of a cPFD filament. During molecular dynamic simulations at 300 and 353 K, each coiled-coil was highly flexible, enabling it to widen the central cavity of the filament to potentially capture various non-native proteins. Docking molecular dynamic simulations of cPFD filaments with unfolded citrate synthase or insulin showed a size-dependence between the substrate and the number of interacting coiled-coils. To confirm this observation, we generated filaments containing specific numbers of subunits, and showed that between six and eight cPFD subunits are required for chaperone activity to prevent citrate synthase from thermal aggregation. These results provide insights into structure-function relationships of oligomeric chaperones and illuminate the potential role of cPFD in its native environment.

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Section: Docking Of Non-native Protein Substrates To Cpfd Filamentssupporting

confidence: 57%

Section: Determining the Minimal Length Of Cpfd Filaments For Chaperosupporting

confidence: 57%

Oligomeric assembly is required for chaperone activity of the filamentous γ‐prefoldin

Glover

Clark

2015

The FEBS Journal

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“…The crystals obtained from the crystallization of PFDα2-β2 yielded only crystals of PFDβ2, similar to the case of PFDα2-β1. 21 Thus, the complexes likely dissociated in the crystallization solution.…”

Section: Resultsmentioning

confidence: 99%

Thermodynamic Characterization of the Interaction between Prefoldin and Group II Chaperonin

Sahlan

Zako

Tai

et al. 2010

Journal of Molecular Biology

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“…In addition, as complete genome sequences of three Pyrococcus species became available at a relatively early stage, members of the Thermococcales have been utilized to study a wide range of archaeal biology. These include DNA replication and repair (Hopkins & Paull, 2008;Williams et al, 2008;Yoshimochi et al, 2008;Kiyonari et al, 2009;Mayanagi et al, 2009;Nishida et al, 2009), transcription and its regulation (Vierke et al, 2003;Lee et al, 2005Lee et al, , 2007Goede et al, 2006;Kanai et al, 2007;Santangelo et al, 2007;Hirata et al, 2008a), carbon and energy metabolism (Sapra et al, 2003;Verhees et al, 2003;Siebers & Schönheit, 2005), CRISPR systems (Hale et al, 2009), and cellular responses to stress, such as oxidative (Jenney et al, 1999;Clay et al, 2003), osmotic (Neves et al, 2005;Rodrigues et al, 2007), and temperature stress (Laksanalamai & Robb, 2004;Danno et al, 2008;Fujiwara et al, 2008;Kanzaki et al, 2008;Kida et al, 2008). The abundant genome sequences have also promoted a wealth of '-omics' research including transcriptomics Lee et al, 2006;Trauger et al, 2008), proteomics , structural genomics (Hura et al, 2009), and other genome-based high-throughput strategies (Keese et al, 2010).…”

Section: Why Study Thermococcales?mentioning

confidence: 99%

Model organisms for genetics in the domain Archaea: methanogens, halophiles,ThermococcalesandSulfolobales

et al. 2011

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The tree of life is split into three main branches: eukaryotes, bacteria, and archaea. Our knowledge of eukaryotic and bacteria cell biology has been built on a foundation of studies in model organisms, using the complementary approaches of genetics and biochemistry. Archaea have led to some exciting discoveries in the field of biochemistry, but archaeal genetics has been slow to get off the ground, not least because these organisms inhabit some of the more inhospitable places on earth and are therefore believed to be difficult to culture. In fact, many species can be cultivated with relative ease and there has been tremendous progress in the development of genetic tools for both major archaeal phyla, the Euryarchaeota and the Crenarchaeota. There are several model organisms available for methanogens, halophiles, and thermophiles; in the latter group, there are genetic systems for Sulfolobales and Thermococcales. In this review, we present the advantages and disadvantages of working with each archaeal group, give an overview of their different genetic systems, and direct the neophyte archaeologist to the most appropriate model organism.

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Structural and Molecular Characterization of the Prefoldin β Subunit from Thermococcus Strain KS-1

Cited by 25 publications

References 34 publications

Oligomeric assembly is required for chaperone activity of the filamentous γ‐prefoldin

Oligomeric assembly is required for chaperone activity of the filamentous γ‐prefoldin

Thermodynamic Characterization of the Interaction between Prefoldin and Group II Chaperonin

Model organisms for genetics in the domain Archaea: methanogens, halophiles,ThermococcalesandSulfolobales

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