http://www.cnr.it/ontology/cnr/individuo/prodotto/ID292459

AtPDIL5-1, an ER-resident putative thiol-disulfide oxidoreductase (Abstract/Poster in convegno)

Type

Label

AtPDIL5-1, an ER-resident putative thiol-disulfide oxidoreductase (Abstract/Poster in convegno) (literal)

Anno

Alternative label

Anna Paola Casazza, William Remelli, Aldo Grasso and Aldo Ceriotti (2014)
AtPDIL5-1, an ER-resident putative thiol-disulfide oxidoreductase
in XVII ENPER Meeting, Roca Vecchia - Melendungno (Lecce), 8-11/09/2014
(literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

Note

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni

Institute of Agricultural Biology and Biotechnology (IBBA), National Research Council (CNR), Via Bassini 15, 20133 Milano, Italy (literal)

Titolo

Abstract

Thiol-disulfide oxidoreductases are the principal actors of oxidative protein folding in the endoplasmic reticulum (ER)1. Due to the presence of at least one thioredoxin (TRX) domain containing the catalytic active CXXC motif, these proteins belong to the TRX superfamily. As ER resident proteins they also possess an N-terminal signal sequence and a C-terminal ER retention signal2. The most extensively studied member is PDI, Protein Disulfide Isomerase, which catalyzes the formation, reduction and isomerization of disulfide bonds and assists polypeptide folding1. The main differences among the PDI-like (PDIL) proteins essentially lie in the number and the position of TRX modules, in the active site sequence and in the presence of additional protein domains3. To date, only few studies have been performed to understand the physiological role of plant ER oxidoreductases, with the most documented function being their involvement in seed germination and development4. Here we present a preliminary characterization of the expression profile and the subcellular localization of AtPDIL5-1, a single TRX-domain PDIL protein from Arabidopsis thaliana. (literal)

Prodotto di

Autore CNR

Prodotto

Autore CNR di

data.CNR.it