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http://purl.uniprot.org/citations/20525253http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20525253http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20525253http://www.w3.org/2000/01/rdf-schema#comment"

Background

The Protein Disulfide Isomerase (PDI) gene family encodes several PDI and PDI-like proteins containing thioredoxin domains and controlling diversified metabolic functions, including disulfide bond formation and isomerisation during protein folding. Genomic, cDNA and promoter sequences of the three homologous wheat genes encoding the "typical" PDI had been cloned and characterized in a previous work. The purpose of present research was the cloning and characterization of the complete set of genes encoding PDI and PDI like proteins in bread wheat (Triticum aestivum cv Chinese Spring) and the comparison of their sequence, structure and expression with homologous genes from other plant species.

Results

Eight new non-homologous wheat genes were cloned and characterized. The nine PDI and PDI-like sequences of wheat were located in chromosome regions syntenic to those in rice and assigned to eight plant phylogenetic groups. The nine wheat genes differed in their sequences, genomic organization as well as in the domain composition and architecture of their deduced proteins; conversely each of them showed high structural conservation with genes from other plant species in the same phylogenetic group. The extensive quantitative RT-PCR analysis of the nine genes in a set of 23 wheat samples, including tissues and developmental stages, showed their constitutive, even though highly variable expression.

Conclusions

The nine wheat genes showed high diversity, while the members of each phylogenetic group were highly conserved even between taxonomically distant plant species like the moss Physcomitrella patens. Although constitutively expressed the nine wheat genes were characterized by different expression profiles reflecting their different genomic organization, protein domain architecture and probably promoter sequences; the high conservation among species indicated the ancient origin and diversification of the still evolving gene family. The comprehensive structural and expression characterization of the complete set of PDI and PDI-like wheat genes represents a basis for the functional characterization of this gene family in the hexaploid context of bread wheat."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.org/dc/terms/identifier"doi:10.1186/1471-2229-10-101"xsd:string
http://purl.uniprot.org/citations/20525253http://purl.org/dc/terms/identifier"doi:10.1186/1471-2229-10-101"xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Ciaffi M."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Ciaffi M."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Dhanapal A.P."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Dhanapal A.P."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Paolacci A.R."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Paolacci A.R."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Porceddu E."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Porceddu E."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Tanzarella O.A."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"Tanzarella O.A."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"d'Aloisio E."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/author"d'Aloisio E."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/date"2010"xsd:gYear
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/name"BMC Plant Biol."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/name"BMC Plant Biol."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/pages"101"xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/pages"101"xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/title"The protein disulfide isomerase gene family in bread wheat (T. aestivum L.)."xsd:string
http://purl.uniprot.org/citations/20525253http://purl.uniprot.org/core/title"The protein disulfide isomerase gene family in bread wheat (T. aestivum L.)."xsd:string
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