Chaperone-Like Activity of Protein Disulfide-Isomerase in the Refolding Of Rhodanese

Song, Jiu-li; Wang, Chih-chen

doi:10.1111/j.1432-1033.1995.tb20702.x

Cited by 136 publications

(61 citation statements)

References 32 publications

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“…Similar results were obtained for rhodanese (Song and Wang, 1995). When the active-site cysteine residues were inactivated by alkylating agents, PDI lost its ability to form and rearrange disulphide bonds.…”

Section: Hydrophobic Interactions Are Essential For Peptide Bindingsupporting

confidence: 73%

Interactions Between Protein Disulphide Isomerase and Peptides

Klappa

Hawkins

Freedman

1997

European Journal of Biochemistry

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There is growing evidence that protein disulphide isomerase (PDI) has a common chaperone function in the endoplasmic reticulum. To characterise this function, we investigated the interaction of purified PDI with radiolabelled model peptides, somatostatin and mastoparan, by cross-linking. The interaction between the peptides and PDI was specific, for it showed saturation and was abolished by denaturation of PDI. The interaction between a hydrophobic peptide without cysteine residues was much more sensitive to Triton X-100 than the interaction between PDI and a more hydrophilic peptide with or without cysteine residues. We therefore propose that hydrophobic interactions between protein disulphide isomerase and peptides play an important role in the binding process. The interaction between PDI and the bound peptide therefore is enhanced by the formation of mixed disulphide bonds.

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Section: Hydrophobic Interactions Are Essential For Peptide Bindingsupporting

confidence: 73%

Interactions Between Protein Disulphide Isomerase and Peptides

Klappa

Hawkins

Freedman

1997

European Journal of Biochemistry

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“…Changes in insulin turbidity were measured for 20 min at 650 nm in a kinetic microplate reader. Chaperone activity of MMTS-modified PDI was determined by rhodanese aggregation assay with the following modifications (46). Rhodanese (1 mg/ml) was first denatured in 5.6 M urea and 10 mM DTT.…”

Section: Methodsmentioning

confidence: 99%

Tissue Factor Coagulant Function Is Enhanced by Protein-disulfide Isomerase Independent of Oxidoreductase Activity

Versteeg

Ruf

2007

Journal of Biological Chemistry

109

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Protein-disulfide isomerase (PDI) switches tissue factor (TF) from coagulation to signaling by targeting the allosteric Cys 186 -Cys 209 disulfide. Here, we further characterize the interaction of purified PDI with TF. We find that PDI enhances factor VIIadependent substrate factor X activation 5-10-fold in the presence of wild-type, oxidized soluble TF but not TF mutants that contain an unpaired Cys 186 or Cys 209 . PDI-accelerated factor Xa generation was blocked by bacitracin but not influenced by inhibition of vicinal thiols, reduction of PDI, changes in redox gradients, or covalent thiol modification of reduced PDI by N-ethylmaleimide or methyl-methanethiosulfonate, which abolished PDI oxidoreductase but not chaperone activity. PDI had no effect on fully active TF on either negatively charged phospholipids or in activating detergent, indicating that PDI selectively acts upon cryptic TF to facilitate ternary complex formation and macromolecular substrate turnover. PDI activation was reduced upon mutation of TF residues in proximity to the macromolecular substrate binding site, consistent with a primary interaction of PDI with TF. PDI enhanced TF coagulant activity on microvesicles shed from cells, suggesting that PDI plays a role as an activating chaperone for circulating cryptic TF.

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“…Chaperone activity was determined as described previously (Song & Wang, 1995). Analysis of mixed disulphides between ERp44 and endogenous client proteins.…”

Section: Methodsmentioning

confidence: 99%

Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy‐terminal tail

Wang

Vavassori

et al. 2008

EMBO Reports

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ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif. Here, we present its crystal structure at a resolution of 2.6 Å . Three thioredoxin domains-a, b and b 0 -are arranged in a clover-like structure. A flexible carboxy-terminal tail turns back to the b 0 and a domains, shielding a hydrophobic pocket in domain b 0 and a hydrophobic patch around the CRFS motif in domain a. Mutational and functional studies indicate that the C-terminal tail gates the CRFS area and the adjacent hydrophobic pocket, dynamically regulating protein quality control.

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Chaperone-Like Activity of Protein Disulfide-Isomerase in the Refolding Of Rhodanese

Cited by 136 publications

References 32 publications

Interactions Between Protein Disulphide Isomerase and Peptides

Interactions Between Protein Disulphide Isomerase and Peptides

Tissue Factor Coagulant Function Is Enhanced by Protein-disulfide Isomerase Independent of Oxidoreductase Activity

Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy‐terminal tail

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