Molecular cloning and characterization of two soybean protein disulfide isomerases as molecular chaperones for seed storage proteins

Kamauchi, Shinya; Wadahama, Hiroyuki; Iwasaki, Kensuke; Nakamoto, Yuya; Nishizawa, Keito; Ishimoto, Masao; Kawada, Teruo; Urade, Reiko

doi:10.1111/j.1742-4658.2008.06412.x

Cited by 43 publications

(53 citation statements)

References 53 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Studies on the rice mutant esp2 (endosperm storage protein 2), which exhibits unusually partitioned proteins and PBs, confirmed the causative role of PDI in the assortment of prolamins and proglutelins, as the mutant lacked the transcripts of PDI (OsPDIL1-1; LOC Os11g09280) (Takemoto et al 2002). Many soybean PDIs also function in storage protein folding and ER stress response, through enzymatic and chaperone activities and/or degradation of unfolded proteins Kamauchi et al 2008;Iwasaki et al 2009). …”

Section: Introductionmentioning

confidence: 97%

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

Dorse

Bhave

2012

Biologia

View full text Add to dashboard Cite

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.

show abstract

Section: Introductionmentioning

confidence: 97%

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

Dorse

Bhave

2012

Biologia

View full text Add to dashboard Cite

show abstract

“…This family of proteins have ubiquitous expression across soybean tissues, are localized to the ER lumen in other tissues and are involved in the proper folding and quality control of storage proteins (71). Import of proteins into the symbiosome would likely require the same processes and, as the structure and composition of the SM is most closely related to the ER (3), these PDI proteins may have been co-opted for this role during the symbiosis.…”

Section: Soybean Symbiosome Proteomementioning

confidence: 99%

Proteomic Analysis of the Soybean Symbiosome Identifies New Symbiotic Proteins*

Clarke

Loughlin

Gavrin

et al. 2015

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Legumes form a symbiosis with rhizobia in which the plant provides an energy source to the rhizobia bacteria that it uses to fix atmospheric nitrogen. This nitrogen is provided to the legume plant, allowing it to grow without the addition of nitrogen fertilizer. As part of the symbiosis, the bacteria in the infected cells of a new root organ, the nodule, are surrounded by a plant-derived membrane, the symbiosome membrane, which becomes the interface between the symbionts. Fractions containing the symbiosome membrane (SM) and material from the lumen of the symbiosome (peribacteroid space or PBS) were isolated from soybean root nodules and analyzed using nongel proteomic techniques. Bicarbonate stripping and chloroform-methanol extraction of isolated SM were used to reduce complexity of the samples and enrich for hydrophobic integral membrane proteins. One hundred and ninety-seven proteins were identified as components of the SM, with an additional fifteen proteins identified from peripheral membrane and PBS protein fractions. Proteins involved in a range of cellular processes such as metabolism, protein folding and degradation, membrane trafficking, and solute transport were identified. These included a number of proteins previously localized to the SM, such as aquaglyceroporin nodulin 26, sulfate transporters, remorin, and Rab7 homologs. Among the proteome were a number of putative transporters for compounds such as sulfate, calcium, hydrogen ions, peptide/ dicarboxylate, and nitrate, as well as transporters for which the substrate is not easy to predict. Analysis of the promoter activity for six genes encoding putative SM proteins showed nodule specific expression, with five showing expression only in infected cells. Localization of two proteins was confirmed using GFP-fusion experiments. The data have been deposited to the ProteomeXchange with identifier PXD001132. This proteome will provide a rich resource for the study of the legumerhizobium symbiosis. Molecular & Cellular Proteomics

show abstract

“…Protein disulfide isomerases play important roles in the formation of disulfide bonds in nascent proteins. Kamauchi et al (2008) characterized two PDILs in soybean (GmPDIL-1 and GmPDIL-2) that were suggested to be molecular chaperones involved in proper folding or quality of legumins. This may suggest a role for Lotus PDILs in disulfide bond formation in the LLPs.…”

Section: Protein Identificationsmentioning

confidence: 99%

The Proteome of Seed Development in the Model Legume Lotus japonicus

et al. 2009

View full text Add to dashboard Cite

We have characterized the development of seeds in the model legume Lotus japonicus. Like soybean (Glycine max) and pea (Pisum sativum), Lotus develops straight seed pods and each pod contains approximately 20 seeds that reach maturity within 40 days. Histological sections show the characteristic three developmental phases of legume seeds and the presence of embryo, endosperm, and seed coat in desiccated seeds. Furthermore, protein, oil, starch, phytic acid, and ash contents were determined, and this indicates that the composition of mature Lotus seed is more similar to soybean than to pea. In a first attempt to determine the seed proteome, both a two-dimensional polyacrylamide gel electrophoresis approach and a gel-based liquid chromatography-mass spectrometry approach were used. Globulins were analyzed by two-dimensional polyacrylamide gel electrophoresis, and five legumins, LLP1 to LLP5, and two convicilins, LCP1 and LCP2, were identified by matrix-assisted laser desorption ionization quadrupole/time-of-flight mass spectrometry. For two distinct developmental phases, seed filling and desiccation, a gel-based liquid chromatography-mass spectrometry approach was used, and 665 and 181 unique proteins corresponding to gene accession numbers were identified for the two phases, respectively. All of the proteome data, including the experimental data and mass spectrometry spectra peaks, were collected in a database that is available to the scientific community via a Web interface (http://www.cbs.dtu.dk/cgi-bin/lotus/db.cgi). This database establishes the basis for relating physiology, biochemistry, and regulation of seed development in Lotus. Together with a new Web interface (http:// bioinfoserver.rsbs.anu.edu.au/utils/PathExpress4legumes/) collecting all protein identifications for Lotus, Medicago, and soybean seed proteomes, this database is a valuable resource for comparative seed proteomics and pathway analysis within and beyond the legume family.

show abstract

Molecular cloning and characterization of two soybean protein disulfide isomerases as molecular chaperones for seed storage proteins

Cited by 43 publications

References 53 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

Proteomic Analysis of the Soybean Symbiosome Identifies New Symbiotic Proteins*

The Proteome of Seed Development in the Model Legume Lotus japonicus

Contact Info

Product

Resources

About