Cloning and characterization of wheat PDI (protein disulfide isomerase) homoeologous genes and promoter sequences

Ciaffi, M.; Paolacci, Anna Rita; d'Aloisio, Elisa; Tanzarella, O. A.; Porceddu, E.

doi:10.1016/j.gene.2005.07.032

Cited by 34 publications

(42 citation statements)

References 32 publications

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“…Interestingly, rice and wheat comprise the most important cereal crops in the world, and the crop yield and grain quality are highly reliant on quality control of seed storage protein deposition. However, there is limited understanding as yet on the contribution of PDI in wheat, except for the reports from our laboratory (Johnson et al 2001;Johnson & Bhave 2004) and others (Ciaffi et al 2006) of the three homologous genes on group 4 chromosomes, and recent report of eight non-homologous groups of genes including TaPDIL2-1 on group 6 chromosomes, TaPDIL3-1 on group 7, TaPDIL4-1 on group 1, TaPDIL5-1 on group 5, TaPDIL6-1 on group 4, TaPDIL7-1 on group 2, and TaPDIL7-2 on group 6 chromosomes (d'Aloisio et al 2010). The present work uses computational tools to identify the complete PDIL gene families in rice and wheat, analyse the encoded proteins products, predict the physical locations of the wheat genes, and identify new candidates with potentially important roles.…”

Section: Introductionmentioning

confidence: 93%

In silico identification and analysis of the protein disulphide isomerases in wheat and rice

Dorse

Bhave

2012

Biologia

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The protein disulphide isomerases (PDI) typically catalyse the formation and isomerization of disulphide bonds during the folding of nascent proteins. Some PDI isoforms may also have chaperone roles under house-keeping and/or stress conditions. Human PDIs and PDI-like (PDIL) proteins show a diverse array of catalytic and chaperone roles. However, understanding of the diversity and roles of plant PDILs is limited. This work aimed to identify the PDIL superfamilies in the two main cereals, rice and wheat, to identify candidates with potential roles in seed storage protein deposition and stress response processes. Searches of the rice genomic and wheat transcript assembly databases, with the Arabidopsis PDILs as queries, led to the identification of twenty two genomic loci in rice, encoding up to thirty two putative coding sequences, as well as twenty expressed sequence tags in wheat. The gene structures in rice ranged from 3 to 15 exons, the exon lengths ranging from 22 to 1,054 base pairs (bp) and the intron lengths from 74 to 1345 bp. The wheat TAs ranged from 584-2,444 bp and many sequences appeared to be orthologous to some of the rice loci. The putative proteins of both plants exhibited the characteristic thioredoxin active-site motif WCXXC, but significant diversity in the lengths of putative proteins and the composition or positions of functional domains therein. The PDILs thus fell into five major groups: PDIL1 (7 in rice; 4 in wheat); PDIL2 (9 rice; 4 wheat); PDIL5 (7 rice; 10 wheat); QSOXL (2 rice; 1 wheat); APRL (7 rice; 1 wheat). The analysis of the gene and putative protein sequences, the functional domains of the latter, and comparisons to literature have led to identification of a number of sequences with potential enzymatic and/or chaperone roles. Several of these appear to be candidates for key roles in seed storage protein folding, plant development and stress response processes in these important crops.

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Section: Introductionmentioning

confidence: 93%

In silico identification and analysis of the protein disulphide isomerases in wheat and rice

Dorse

Bhave

2012

Biologia

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“…A high degree of conservation was found within the RPL3-family with similarities among homoeologous genes that are slightly higher than reported from studies with other genes from wheat: similarity among the RPL3 homoeologs lies between 97.3 and 98.7%, while cDNA sequences of the Waxy granule-bound starch synthase homoeologs are about 96% similar (Murai et al 1999), that of the wknox1 (orthologs of the KNOTTED1 homeobox protein from maize) about 95% (Takumi et al 2000), and PDI (protein disulWde isomerase) homoeologous genes show 96-97.5% identity (CiaY et al 2005).…”

Section: Discussionmentioning

confidence: 83%

Cloning and characterization of the ribosomal protein L3 (RPL3) gene family from Triticum aestivum

et al. 2007

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Plant pathogenic fungi of the genus Fusarium can cause severe diseases on small grain cereals and maize. The contamination of harvested grain with Fusarium mycotoxins is a threat to human and animal health. In wheat production of the toxin deoxynivalenol (DON), which inhibits eukaryotic protein biosynthesis, is a virulence factor of Fusarium, and resistance against DON is considered to be part of Fusarium resistance. Previously, single amino acid changes in RPL3 (ribosomal protein L3) conferring DON resistance have been described in yeast. The goal of this work was to characterize the RPL3 gene family from wheat and to investigate the potential role of naturally existing RPL3 alleles in DON resistance by comparing Fusarium-resistant and susceptible cultivars. The gene family consists of three homoeologous alleles of both RPL3A and RPL3B, which are located on chromosomes 4A

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“…The nucleotide sequences of the three genes located respectively on genomes A, B, and D (designed as GPDI-4A, GPDI-4B and GPDI-4D) were 3561 bp, 3527 bp and 3466 bp long. The comparison of typical PDI gene sequences of wheat, rice and Arabidopsis showed a significant conservation of the exon/intron structure across the three species [31]. More detailed study on the complexity and diversity of the genes encoding PDI and PDI-like proteins in wheat and other plant species also showed a significant conservation of the exon/intron structure [28].…”

Section: Introductionmentioning

confidence: 92%

“…The PDI-4A transcription was higher in spikelets, that of PDI-4B were higher in roots while the PDI-4 D transcripts were more abundant in leaves. The transcripttion levels of the three genes were higher in the early stage of seed development (6 -14 DAA) and decreased during middle to late stage of (18 -34 DAA) grain filling [31]. Within the upstream putative promoter region of the three homoeologous genes cloned from bread wheat cv CS, respectively 1352 bp for PromPDI-4A, 1370 bp for PromPDI-4B and 1292 bp for PromPDI-4D long, several cis-acting elements involved in endosperm specific expression were detected, consistently with the higher PDI expression detected in the kernels.…”

Section: Introductionmentioning

confidence: 94%

“…Chinese Spring (CS) (Ciaffi et al, 2006) showed that the PDI transcripts, although constitutively present at a low level in all the analyzed tissues, are equally abundant in the developing caryopses but are differentially expressed in spikelets, roots and leaves [25,31]. The PDI-4A transcription was higher in spikelets, that of PDI-4B were higher in roots while the PDI-4 D transcripts were more abundant in leaves.…”

Section: Introductionmentioning

confidence: 99%

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Evolutionary Relationship of Wheat Protein Disulphide Isomerase (PDI) Gene Promoter Sequence Based on Phylogenetic Analysis

Dhanapal¹

2012

AJPS

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Protein disulphide isomerase (PDI) is an oxidoreductase enzyme abundant in the endoplasmic reticulum (ER). In plants, PDIs have been shown to assist the folding and deposition of seed storage proteins during the biogenesis of protein bodies in the endosperm. 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 were reported in our previous publications. Promoter sequences of three homoeologous genes encoding typical PDI, located on chromosome group 4 of bread wheat, and PDI promoter sequence analysis of Triticum urartu, Aegilops speltoides and Aegilops tauschii had also been reported previously. In this study, we report the isolation and sequencing of a ~700 bp region, comprising ~600 bp of the putative promoter region and 88 bp of the first exon of the typical PDI gene, in five accessions each from Triticum urartu (AA), Aegilops speltoides (BB) and Aegilops tauschii (DD). Sequence analysis indicated large variation among sequences belonging to the different genomes, while close similarity was found within each species and with the corresponding homoeologous PDI sequences of Triticum aestivum cv. CS (AABBDD) resulting in an overall high conservation of the sequence conferring endosperm-specific expression.

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Cloning and characterization of wheat PDI (protein disulfide isomerase) homoeologous genes and promoter sequences

Cited by 34 publications

References 32 publications

In silico identification and analysis of the protein disulphide isomerases in wheat and rice

In silico identification and analysis of the protein disulphide isomerases in wheat and rice

Cloning and characterization of the ribosomal protein L3 (RPL3) gene family from Triticum aestivum

Evolutionary Relationship of Wheat Protein Disulphide Isomerase (PDI) Gene Promoter Sequence Based on Phylogenetic Analysis

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