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

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