scholarly journals Acid-Denatured Green Fluorescent Protein (GFP) as Model Substrate to Study the Chaperone Activity of Protein Disulfide Isomerase

2011 ◽  
Vol 12 (7) ◽  
pp. 4625-4636 ◽  
Author(s):  
Rosa E. Mares ◽  
Samuel G. Meléndez-López ◽  
Marco A. Ramos
Keyword(s):  
Green Fluorescent Protein ◽  
Protein Disulfide Isomerase ◽  
Fluorescent Protein ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Green Fluorescent ◽  
Protein Disulfide

scholarly journals Identification of a Novel Saturable Endoplasmic Reticulum Localization Mechanism Mediated by the C-Terminus of aDictyostelium Protein Disulfide Isomerase

2000 ◽  
Vol 11 (10) ◽  
pp. 3469-3484 ◽  
Author(s):  
Jean Monnat ◽  
Eva M. Neuhaus ◽  
Marius S. Pop ◽  
David M. Ferrari ◽  
Barbara Kramer ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Fluorescent Protein ◽  
Null Mutation ◽  
Disulfide Isomerase ◽  
Isomerase Activity ◽  
C Terminus ◽  
Complementary Action ◽  
Green Fluorescent ◽  
Protein Disulfide

Localization of soluble endoplasmic reticulum (ER) resident proteins is likely achieved by the complementary action of retrieval and retention mechanisms. Whereas the machinery involving the H/KDEL and related retrieval signals in targeting escapees back to the ER is well characterized, other mechanisms including retention are still poorly understood. We have identified a protein disulfide isomerase (Dd-PDI) lacking the HDEL retrieval signal normally found at the C terminus of ER residents in Dictyostelium discoideum. Here we demonstrate that its 57 residue C-terminal domain is necessary for intracellular retention of Dd-PDI and sufficient to localize a green fluorescent protein (GFP) chimera to the ER, especially to the nuclear envelope. Dd-PDI and GFP-PDI57 are recovered in similar cation-dependent complexes. The overexpression of GFP-PDI57 leads to disruption of endogenous PDI complexes and induces the secretion of PDI, whereas overexpression of a GFP-HDEL chimera induces the secretion of endogenous calreticulin, revealing the presence of two independent and saturable mechanisms. Finally, low-level expression of Dd-PDI but not of PDI truncated of its 57 C-terminal residues complements the otherwise lethal yeast TRG1/PDI1 null mutation, demonstrating functional disulfide isomerase activity and ER localization. Altogether, these results indicate that the PDI57 peptide contains ER localization determinants recognized by a conserved machinery present in D. discoideum and Saccharomyces cerevisiae.

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 DsbG, a Protein Disulfide Isomerase with Chaperone Activity

2000 ◽  
Vol 275 (18) ◽  
pp. 13349-13352 ◽  
Author(s):  
Feng Shao ◽  
Martin W. Bader ◽  
Ursula Jakob ◽  
James C. A. Bardwell
Keyword(s):  
Protein Disulfide Isomerase ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Ribostamycin Inhibits the Chaperone Activity of Protein Disulfide Isomerase

2001 ◽  
Vol 289 (5) ◽  
pp. 967-972 ◽  
Author(s):  
Tomohisa Horibe ◽  
Hiroaki Nagai ◽  
Keiichi Sakakibara ◽  
Yasunari Hagiwara ◽  
Masakazu Kikuchi
Keyword(s):  
Protein Disulfide Isomerase ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Protein Disulfide
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