Please use this identifier to cite or link to this item:
http://hdl.handle.net/2067/1619
Title: | The PDI (Protein Disulfide Isomerase) gene family in wheat. | Authors: | d'Aloisio, Elisa Tanzarella, Oronzo A. Dhanapal, Arun Prabhu Porceddu, Enrico Ciaffi, Mario |
Keywords: | Protein Disulfide Isomerase;Disolfuro isomerasi;Wheat;Frumento;Gene cloning and characterization;Clonazione e caratterizzazione di geni | Issue Date: | 2008 | Publisher: | Sydney University Press | Source: | d'Aloisio, E. et al. 2008. The PDI (Protein Disulfide Isomerase) gene family in wheat. In: Appels R. et al. (eds). Proceedings of the 11th International Wheat Genetics Symposium. (Brisbane, Australia 24-29 August 2008) 1-3. | Abstract: | The PDI (Protein Disulfide Isomerase) gene family includes several members whose products are responsible for diversified metabolic functions. PDI and PDI-like proteins differ for number and position of thioredoxin-like (TRX-like) active (a type) and inactive (b type) domains, for presence/absence of other domains and of the KDEL signal of retention in the endoplasmic reticulum (ER). The phylogenetic analysis of typical PDI and PDI-like protein sequences resolved them into 10 groups (1), 5 of them (I-V) had 2 TRX-like active domains, whereas the remaining ones owned only a single TRX-like active domain (VI-VIII, QSOX and APRL). In particular, QRX and APRL were not included in this study due to their putative non-isomerase enzymatic activities encoded by an additional domain. The aim of the present research was the study of the complexity and diversity of the PDI gene family in wheat, with particular focus on the genes encoding PDIlike proteins structurally similar to TaPDIL1-1 (group I), the first identified and best characterized member of the PDI family, also named typical PDI. The most important function of typical PDI is the formation and isomerization of disulfide bonds during protein folding, which are accomplished by its two active TRX-like sites sharing the characteristic tetrapeptide –CGHC-. Several studies of molecular characterization, expression analysis and cell localisation in rice and maize have suggested the involvement of typical PDI in the assembly and deposition of storage proteins in these species (2, 3, 4). The characterization and chromosome location of the three homoeologous gene sequences encoding typical PDI and of their promoter sequences have been reported previously (5). |
URI: | http://hdl.handle.net/2067/1619 | ISBN: | 978-1-920899-14-1 |
Appears in Collections: | DABAC - Archivio della produzione scientifica |
Files in This Item:
File | Description | Size | Format | |
---|---|---|---|---|
dAloisio etal PDI IWGS 2008.pdf | 242.73 kB | Adobe PDF | View/Open |
Page view(s)
107
Last Week
0
0
Last month
3
3
checked on Mar 16, 2024
Download(s)
33
checked on Mar 16, 2024
Google ScholarTM
Check
Altmetric
All documents in the "Unitus Open Access" community are published as open access.
All documents in the community "Prodotti della Ricerca" are restricted access unless otherwise indicated for specific documents