Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer

Biochemistry ◽  
1991 ◽  
Vol 30 (3) ◽  
pp. 613-619 ◽  
Author(s):  
Michelle M. Lyles ◽  
Hiram F. Gilbert
Keyword(s):  
Protein Disulfide Isomerase ◽  
Ribonuclease A ◽  
Oxidative Folding ◽  
Disulfide Isomerase ◽  
Protein Disulfide ◽  
Redox Buffer

Oxidative folding and reductive activities of EhPDI, a protein disulfide isomerase from Entamoeba histolytica

2009 ◽  
Vol 58 (3) ◽  
pp. 311-313 ◽  
Author(s):  
Rosa E. Mares ◽  
Paloma D. Magaña ◽  
Samuel G. Meléndez-López ◽  
Alexei F. Licea ◽  
José M. Cornejo-Bravo ◽  
...  
Keyword(s):  
Entamoeba Histolytica ◽  
Protein Disulfide Isomerase ◽  
Oxidative Folding ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Oxidative Folding of Conopeptides Modified by Conus Protein Disulfide Isomerase

2017 ◽  
Vol 36 (5) ◽  
pp. 407-416 ◽  
Author(s):  
Lei Wang ◽  
Xiaomin Wang ◽  
Zhenghua Ren ◽  
Wei Tang ◽  
Qiong Zou ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Oxidative Folding ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Reconstitution of Human Ero1-Lα/Protein-Disulfide Isomerase Oxidative Folding Pathwayin Vitro

2008 ◽  
Vol 284 (1) ◽  
pp. 199-206 ◽  
Author(s):  
Lei Wang ◽  
Sheng-jian Li ◽  
Ateesh Sidhu ◽  
Li Zhu ◽  
Yi Liang ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Oxidative Folding ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Functional analysis of tunicamycin-inducible gene A polypeptide from Aspergillus niger

2005 ◽  
Vol 83 (5) ◽  
pp. 654-658 ◽  
Author(s):  
Yurong Liang ◽  
Wei Li ◽  
Qing Ma ◽  
Yuying Zhang
Keyword(s):  
Functional Analysis ◽  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Protein Disulfide Isomerase ◽  
Ribonuclease A ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Chaperone Protein ◽  
Protein Disulfide ◽  
Inducible Gene

Tunicamycin-inducible gene A polypeptide (TIGA) is a member of the protein disulfide isomerase (PDI) family and is suggested to facilitate the folding of nascent polypeptides. The functional properties of TIGA were investigated here. TIGA acted as an isomerase, catalyzing the refolding of denatured and reduced ribonuclease A. TIGA also exhibited chaperone activity in the refolding of denatured prochymosin but not in the refolding of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), indicating that it had substrate specificity with respect to chaperone activity. Detailed study with a series of thioredoxin-motif (trx-motif) mutants revealed that the 2 trx-motifs of TIGA were not equal in activity. The N-terminal trx-motif was more active than the C-terminal trx-motif, and the first cysteine in each trx-motif was necessary for isomerase activity.Key words: tunicamycin-inducible gene A polypeptide (TIGA), protein disulfide isomerase, chaperone, protein refolding.

scholarly journals Mutations in domaina′ of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A

2003 ◽  
Vol 12 (5) ◽  
pp. 939-952 ◽  
Author(s):  
Margherita Ruoppolo ◽  
Stefania Orrù ◽  
Fabio Talamo ◽  
Johanna Ljung ◽  
Annamari Pirneskoski ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Ribonuclease A ◽  
Folding Pathway ◽  
Disulfide Isomerase ◽  
Pancreatic Ribonuclease ◽  
Pancreatic Ribonuclease A ◽  
Protein Disulfide

scholarly journals Functional Relationship between Protein Disulfide Isomerase Family Members during the Oxidative Folding of Human Secretory Proteins

2010 ◽  
Vol 21 (18) ◽  
pp. 3093-3105 ◽  
Author(s):  
Lori A. Rutkevich ◽  
Myrna F. Cohen-Doyle ◽  
Ulf Brockmeier ◽  
David B. Williams
Keyword(s):  
Protein Disulfide Isomerase ◽  
High Efficiency ◽  
Family Members ◽  
Secretory Proteins ◽  
Human Hepatoma Cells ◽  
Oxidative Folding ◽  
Disulfide Isomerase ◽  
The Impact ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family

To examine the relationship between protein disulfide isomerase family members within the mammalian endoplasmic reticulum, PDI, ERp57, ERp72, and P5 were depleted with high efficiency in human hepatoma cells, either singly or in combination. The impact was assessed on the oxidative folding of several well-characterized secretory proteins. We show that PDI plays a predominant role in oxidative folding because its depletion delayed disulfide formation in all secretory proteins tested. However, the phenotype was surprisingly modest suggesting that other family members are able to compensate for PDI depletion, albeit with reduced efficacy. ERp57 also exhibited broad specificity, overlapping with that of PDI, but with preference for glycosylated substrates. Depletion of both PDI and ERp57 revealed that some substrates require both enzymes for optimal folding and, furthermore, led to generalized protein misfolding, impaired export from the ER, and degradation. In contrast, depletion of ERp72 or P5, either alone or in combination with PDI or ERp57 had minimal impact, revealing a narrow substrate specificity for ERp72 and no detectable role for P5 in oxidative protein folding.

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