NDLI: Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

Please wait, while we are loading the content...

Cytoplasmic domains of the common beta-chain of the GM-CSF/IL-3/IL-5 receptors that are required for inducing differentiation or clonal suppression in myeloid leukaemic cell lines.

Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI.

Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: a conformational mechanism for SH3 domain regulation.

The mammalian profilin isoforms display complementary affinities for PIP2 and proline-rich sequences.

Transgenic expression in the liver of truncated Met blocks apoptosis and permits immortalization of hepatocytes.

Expression of the papillomavirus E2 protein in HeLa cells leads to apoptosis.

D-mef2 is a target for Tinman activation during Drosophila heart development.

Yeast telomeric sequences function as chromosomal anchorage points in vivo.

Fission yeast pheromone blocks S-phase by inhibiting the G1 cyclin B-p34cdc2 kinase.

Chk1 is a wee1 kinase in the G2 DNA damage checkpoint inhibiting cdc2 by Y15 phosphorylation.

Histone acetyltransferase activity and interaction with ADA2 are critical for GCN5 function in vivo.

Concerted evolution of the tandemly repeated genes encoding human U2 snRNA (the RNU2 locus) involves rapid intrachromosomal homogenization and rare interchromosomal gene conversion.

Viroid processing: switch from cleavage to ligation is driven by a change from a tetraloop to a loop E conformation.

Oncogenic potential of TAR RNA binding protein TRBP and its regulatory interaction with RNA-dependent protein kinase PKR.

Open complex formation around a lesion during nucleotide excision repair provides a structure for cleavage by human XPG protein.

A role for DNA primase in coupling DNA replication to DNA damage response.

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

A small heat shock protein stably binds heat-denatured model substrates and can maintain a substrate in a folding-competent state.

Year: 1997, Volume: 16, Issue: 2

Year: 1997, Volume: 16, Issue: 1

Year: 1996, Volume: 15

Year: 1995, Volume: 14

Year: 1994, Volume: 13

Year: 1993, Volume: 12

Year: 1992, Volume: 11

Year: 1991, Volume: 10

Year: 1990, Volume: 9

Year: 1989, Volume: 8

Year: 1988, Volume: 7

Year: 1987, Volume: 6

Year: 1986, Volume: 5

Year: 1985, Volume: 4

Year: 1984, Volume: 3

Year: 1983, Volume: 2

Year: 1982, Volume: 1

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

Content Provider	PubMed Central
Author	Yao, Y. Zhou, Y. Wang, C.
Abstract	The spontaneous reactivation yield of acidic phospholipase A2 (APLA2), a protein containing seven disulfide bonds, after reduction and denaturation in guanidine hydrochloride is very low. Protein disulfide isomerase (PDI) markedly increases the reactivation yield and prevents the aggregation of APLA2 during refolding in a redox buffer containing GSH and GSSG. S-methylated PDI (mPDI), with no isomerase but as nearly full chaperone activity as native PDI, has no effect on either the reactivation or aggregation of APLA2. However, the simultaneous presence of PDI and mPDI in molar ratios to APLA2 of 0.1 and 0.9 respectively fully reactivates the denatured enzyme, as does PDI alone at a ratio of 1. At ratios of 0.1 and 0.15 respectively, they completely suppress APLA2 aggregation, as does PDI alone at a ratio of 0.25. Moreover, delayed addition of PDI to the refolding buffer greatly diminished the reactivation yield of APLA2, but this deteriorating effect can be alleviated markedly by the presence of mPDI in the refolding buffer. Without GSSG, mPDI prevents the aggregation of APLA2 during refolding. It is proposed that the in vitro action of PDI as a foldase consists of both isomerase and chaperone activities, and the latter activity can be fully replaced by mPDI.
Related Links	http://dx.doi.org/10.1093/emboj/16.3.651
Ending Page	658
Page Count	8
Starting Page	651
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	3
Volume Number	16
Language	English
Publisher Date	1997-02-01
Access Restriction	Open
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

Sl.	Authority	Responsibilities	Communication Details
1	Ministry of Education (GoI), Department of Higher Education	Sanctioning Authority	https://www.education.gov.in/ict-initiatives
2	Indian Institute of Technology Kharagpur	Host Institute of the Project: The host institute of the project is responsible for providing infrastructure support and hosting the project	https://www.iitkgp.ac.in
3	National Digital Library of India Office, Indian Institute of Technology Kharagpur	The administrative and infrastructural headquarters of the project	Dr. B. Sutradhar bsutra@ndl.gov.in
4	Project PI / Joint PI	Principal Investigator and Joint Principal Investigators of the project	Dr. B. Sutradhar bsutra@ndl.gov.in Prof. Saswat Chakrabarti will be added soon
5	Website/Portal (Helpdesk)	Queries regarding NDLI and its services	support@ndl.gov.in
6	Contents and Copyright Issues	Queries related to content curation and copyright issues	content@ndl.gov.in
7	National Digital Library of India Club (NDLI Club)	Queries related to NDLI Club formation, support, user awareness program, seminar/symposium, collaboration, social media, promotion, and outreach	clubsupport@ndl.gov.in
8	Digital Preservation Centre (DPC)	Assistance with digitizing and archiving copyright-free printed books	dpc@ndl.gov.in
9	IDR Setup or Support	Queries related to establishment and support of Institutional Digital Repository (IDR) and IDR workshops	idr@ndl.gov.in

The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.

Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme.

Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor

Is protein disulfide isomerase a redox-dependent molecular chaperone?

Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor.

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

A 21-kDa C-terminal Fragment of Protein-disulfide Isomerase has Isomerase, Chaperone, and Anti-chaperone Activities

The Acidic C-terminal Domain Stabilizes the Chaperone Function of Protein Disulfide Isomerase

The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase.

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.

Similar Documents

The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.

Anti-chaperone behavior of BiP during the protein disulfide isomerase-catalyzed refolding of reduced denatured lysozyme.

Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor

Is protein disulfide isomerase a redox-dependent molecular chaperone?

Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor.

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

A 21-kDa C-terminal Fragment of Protein-disulfide Isomerase has Isomerase, Chaperone, and Anti-chaperone Activities

The Acidic C-terminal Domain Stabilizes the Chaperone Function of Protein Disulfide Isomerase

The role of the thiol/disulfide centers and peptide binding site in the chaperone and anti-chaperone activities of protein disulfide isomerase.

Both the isomerase and chaperone activities of protein disulfide isomerase are required for the reactivation of reduced and denatured acidic phospholipase A2.