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The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)

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...

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Autores principales: d'Aloisio, Elisa, Paolacci, Anna R, Dhanapal, Arun P, Tanzarella, Oronzo A, Porceddu, Enrico, Ciaffi, Mario
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3017771/
https://www.ncbi.nlm.nih.gov/pubmed/20525253
http://dx.doi.org/10.1186/1471-2229-10-101
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author d'Aloisio, Elisa
Paolacci, Anna R
Dhanapal, Arun P
Tanzarella, Oronzo A
Porceddu, Enrico
Ciaffi, Mario
author_facet d'Aloisio, Elisa
Paolacci, Anna R
Dhanapal, Arun P
Tanzarella, Oronzo A
Porceddu, Enrico
Ciaffi, Mario
author_sort d'Aloisio, Elisa
collection PubMed
description 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 homoeologous 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-homoeologous 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.
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spelling pubmed-30177712011-01-10 The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.) d'Aloisio, Elisa Paolacci, Anna R Dhanapal, Arun P Tanzarella, Oronzo A Porceddu, Enrico Ciaffi, Mario BMC Plant Biol Research Article 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 homoeologous 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-homoeologous 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. BioMed Central 2010-06-03 /pmc/articles/PMC3017771/ /pubmed/20525253 http://dx.doi.org/10.1186/1471-2229-10-101 Text en Copyright ©2010 d'Aloisio et al; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Article
d'Aloisio, Elisa
Paolacci, Anna R
Dhanapal, Arun P
Tanzarella, Oronzo A
Porceddu, Enrico
Ciaffi, Mario
The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)
title The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)
title_full The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)
title_fullStr The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)
title_full_unstemmed The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)
title_short The Protein Disulfide Isomerase gene family in bread wheat (T. aestivum L.)
title_sort protein disulfide isomerase gene family in bread wheat (t. aestivum l.)
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3017771/
https://www.ncbi.nlm.nih.gov/pubmed/20525253
http://dx.doi.org/10.1186/1471-2229-10-101
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