FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis–trans isomerase with activities to trap and refold denatured proteins

Ideno, Akira; Yoshida, Takao; Iida, Toshii; Furutani, Masahiro; Maruyama, Tadashi

doi:10.1042/bj3570465

Cited by 26 publications

(23 citation statements)

References 30 publications

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“…The solubility of p53 was drastically improved by TcFKBP18 (lanes 4 and 5, Fig. 5B), agreeing well with the reported ability of this molecular chaperone to trap and refold many heterologous misfolded recombinant proteins (13,35). Further testing of the power and versatility of TcFKBP18 was done in the next application, PIMAX-CoP.…”

Section: Fig 3 Phosphorylation Enhances Tau Fibrillization In Vitrosupporting

confidence: 64%

“…Specifically, we chose TcFKBP18, an FK506-binding protein from the hyperthermophilic archaeon Thermococcus sp. KS-1 (35). Unlike other multicomponent E. coli proteinfolding machinery such as DnaJ/DnaK and GroEL/GroES, TcFKBP18 acts alone to trap and refold denatured proteins in vitro and can increase the solubility of several recombinant proteins in vivo (13) when fused physically to these clients.…”

Section: Fig 3 Phosphorylation Enhances Tau Fibrillization In Vitromentioning

confidence: 99%

“…KS-1 (35). Unlike other multicomponent E. coli proteinfolding machinery such as DnaJ/DnaK and GroEL/GroES, TcFKBP18 acts alone to trap and refold denatured proteins in vitro and can increase the solubility of several recombinant proteins in vivo (13) when fused physically to these clients. Taking advantage of the small size of TcFKBP18, as well as the simplicity of the system's setup, we tested whether this molecular chaperone can facilitate protein solubility in the context of PIMAX-CAF.…”

Section: Fig 3 Phosphorylation Enhances Tau Fibrillization In Vitromentioning

confidence: 99%

“…In contrast to these multicomponent protein folding/disaggregation systems, other proteins exert the molecular chaperone function from within a much smaller ensemble or even without an obligatory cofactor (10). These simpler molecular chaperones include peptidyl prolyl cis-trans isomerase, thioredoxin, and disulfide isomerase dsbA (8,(11)(12)(13) and have been fused to target proteins to act as solubility enhancers. The simple operation and minimal strain manipulation make such molecular chaperones particularly attractive in synthesizing recombinant proteins.…”

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confidence: 99%

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Protein Interaction Module–assisted Function X (PIMAX) Approach to Producing Challenging Proteins Including Hyperphosphorylated Tau and Active CDK5/p25 Kinase Complex

Sui

et al. 2015

Molecular & Cellular Proteomics

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Many biomedically critical proteins are underrepresented in proteomics and biochemical studies because of the difficulty of their production in Escherichia coli. These proteins might possess posttranslational modifications vital to their functions, tend to misfold and be partitioned into bacterial inclusion bodies, or act only in a stoichiometric dimeric complex. Successful production of these proteins requires efficient interaction between these proteins and a specific "facilitator," such as a protein-modifying enzyme, a molecular chaperone, or a natural physical partner within the dimeric complex. Here we report the design and application of a protein interaction moduleassisted function X (PIMAX) system that effectively overcomes these hurdles. By fusing two proteins of interest to a pair of well-studied protein-protein interaction modules, we were able to potentiate the association of these two proteins, resulting in successful production of an enzymatically active cyclin-dependent kinase complex and hyperphosphorylated tau protein, which is intimately linked to Alzheimer disease. Furthermore, using tau isoforms quantitatively phosphorylated by GSK-3␤ and CDK5 kinases via PIMAX, we demonstrated the hyperphosphorylation-stimulated tau oligomerization in vitro, paving the way for new Alzheimer disease drug discoveries. Vectors for PIMAX can be easily modified to meet the needs of different applications. This approach thus provides a convenient and modular suite with broad implications for proteomics and biomedical research. Molecular & Cellular Proteomics

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Section: Fig 3 Phosphorylation Enhances Tau Fibrillization In Vitrosupporting

confidence: 64%

Section: Fig 3 Phosphorylation Enhances Tau Fibrillization In Vitromentioning

confidence: 99%

Section: Fig 3 Phosphorylation Enhances Tau Fibrillization In Vitromentioning

confidence: 99%

mentioning

confidence: 99%

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Protein Interaction Module–assisted Function X (PIMAX) Approach to Producing Challenging Proteins Including Hyperphosphorylated Tau and Active CDK5/p25 Kinase Complex

Sui

et al. 2015

Molecular & Cellular Proteomics

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“…Archaeal FKBPs have been classified into two groups: 16-to 18-kDa FKBPs (short-type FKBPs) and 26-to 33-kDa FKBPs (long-type FKBPs) (20). It has been reported that the short-type FKBP from archaea possesses not only PPIase activity but also chaperone-like protein folding activity in vitro (4,13). The long-type FKBPs consist of an N-terminal FKBP domain, which is homologous to that in the short-type FKBPs, and an adjacent C-terminal domain comprising ca.…”

Section: Fk506 Binding Protein (Fkbp) Is a Family Of Peptidyl-prolylmentioning

confidence: 99%

FK506 Binding Protein from the Hyperthermophilic Archaeon Pyrococcus horikoshii Suppresses the Aggregation of Proteins in Escherichia coli

Ideno

Furutani

Iba

et al. 2002

Appl Environ Microbiol

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The 29-kDa FK506 binding protein (FKBP) gene is the only peptidyl-prolyl cis-trans isomerase (PPIase) gene in the genome of Pyrococcus horikoshii. We characterized the function of this FKBP (PhFKBP29) and used it to increase the production yield of soluble recombinant protein in Escherichia coli. The PPIase activity (k cat /K m ) of PhFKBP29 was found to be much lower than that of other archaeal 16-to 18-kDa FKBPs by a chymotrypsincoupled assay of the oligo-peptidyl substrate at 15°C. Besides this low PPIase activity, PhFKBP29 showed chaperone-like protein folding activity which enhanced the refolding yield of chemically unfolded rhodanese in vitro. In addition, it suppressed thermal protein aggregation in a temperature range of 45 to 100°C. When the PhFKBP29 gene was coexpressed with the recombinant Fab fragment gene of the anti-hen egg lysozyme antibody in the cytoplasm of E. coli, whose expressed product tended to form an inactive aggregate in E. coli, it improved the yield of the soluble Fab fragments with antibody specificity. PhFKBP29 exerted protein folding and aggregation suppression in E. coli cells.

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Characterization of immunophilins in the silkmoth Bombyx mori

Somarelli

Coll

Velandia

et al. 2007

Arch Insect Biochem Physiol

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The FK506-binding proteins (FKBPs) perform an extensive variety of functions in numerous organisms from archaea to humans. The FKBPs are distinguished by their peptidyl-prolyl cis-trans isomerase (PPIase) activity and ability to bind the immunosuppressive drugs FK506 and rapamycin. Here, we report the isolation and characterization of FKBP45, a novel member of the FKBP family obtained from U1 small nuclear RNA (snRNA) binding assays using Bombyx mori nuclear extracts. The protein, an apparent orthologue of FKBP46 from the armyworm, Spodoptera frugiperda, was found to associate with U1 stem-loop I RNA in vitro. The FKBP45 cDNA was isolated and the genomic sequence was characterized, including the positions of exon/intron junctions and consensus splice sites. Using bioinformatics, transcription factor consensus binding sites were identified and subsequent Western blotting from developing eggs indicate that FKBP45 is differentially expressed during embryogenesis. A database was assembled using more than 1,800 available FKBP amino acid sequences and pairwise sequence alignments revealed several putative FKBP45 orthologues in various species. Analysis of these sequences revealed the position of an RNA binding domain within this new protein. In addition, FKBP45 possesses similar characteristics to several potential orthologues, including the presence of bipartite nuclear localization signals (NLSs) and phosphorylation sites.

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FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis–trans isomerase with activities to trap and refold denatured proteins

Abstract: 465 FK506-binding protein of the hyperthermophilic archaeum, Thermococcus sp. KS-1, a cold-shock-inducible peptidyl-prolyl cis-trans isomerase with activities to trap and refold denatured proteins

Cited by 26 publications

References 30 publications

Protein Interaction Module–assisted Function X (PIMAX) Approach to Producing Challenging Proteins Including Hyperphosphorylated Tau and Active CDK5/p25 Kinase Complex

Protein Interaction Module–assisted Function X (PIMAX) Approach to Producing Challenging Proteins Including Hyperphosphorylated Tau and Active CDK5/p25 Kinase Complex

FK506 Binding Protein from the Hyperthermophilic Archaeon Pyrococcus horikoshii Suppresses the Aggregation of Proteins in Escherichia coli

Characterization of immunophilins in the silkmoth Bombyx mori

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