Molecular characterization of a cDNA encoding disulfide isomerase during barley kernel development

Kim, J. Y.; Lee, M. S.; Jang, Cheol Seong; Heo, Hwa‐Young; Park, K. G.; Kim, H. S.; Kang, Man-Jung; Kim, S. J.; Kim, J. G.; Hyun, Dong Yun; Seo, Yong Weon

doi:10.1134/s1021443708050129

Cited by 1 publication

(4 citation statements)

References 27 publications

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“…The results from two independent plant cultures are shown in Fig 5 . Four of five cultivars presented the highest PDI1-1 protein level at the earlier developmental stage (10 DAA), which is in agreement with observations for other barley cultivars [ 35 – 36 ]. However, cultivar 18 showed higher PDI1-1 content at 20 DAA.…”

Section: Resultssupporting

confidence: 90%

“…The grain content was evaluated at 10, 20 and 30 DAA. Selection of these stages aimed to represent grain maturation and dehydration and mirrored the major PDI1-1 transcript fluctuations ( Fig 3 ) and [ 35 ].…”

Section: Resultsmentioning

confidence: 99%

“…The reproducibly different localization of spots corresponding to PDI1-1 in cultivars 04, 11 and 19 compared to 18 and 23, as well as their apparently different accumulation levels, prompted us to more deeply characterize this protein as a potential biomarker in Mexican barley cultivars. PDI1-1 is a major protein disulfide isomerase described in barley and wheat during seed development [ 28 , 35 ]. Several genes coding for PDI and PDI-like (PDIL) proteins have been identified in plants but information about their structural and functional features is still limited, reviewed in [ 41 ].…”

Section: Discussionmentioning

confidence: 99%

“…In rice, the lack of PDIL1-1 has been associated with abnormal accumulation of glutelin precursor, defects in the formation of correct prolamin-containing protein bodies derived from ER and the increased accumulation of many types of seed proteins [ 27 , 43 ]. In barley and wheat, PDI1 (PDIL1) represents the most abundant isoform from the reported family members [ 28 , 35 ]. Its levels and localization are thought to exert major influence on the correct protein folding of prolamins and their distribution in storage protein bodies throughout grain development.…”

Section: Discussionmentioning

confidence: 99%

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Protein Disulfide Isomerase (PDI1-1) differential expression and modification in Mexican malting barley cultivars

et al. 2018

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Barley malting quality depends on seed characteristics achieved during grain development and germination. One important parameter is protein accumulation in the mature seed, which may vary between cultivars. Here we conducted a protein pattern analysis in the range of pI 4–7 of mature grains from five Mexican barley cultivars, commonly used for malt and beer production. Reproducibly distinct protein spots, separated by 2D SDS PAGE, were identified by mass spectrometry and considered as potential markers for cultivars with distinct seed protein accumulation. The expression patterns of glutamate decarboxylase (GAD) and protein disulfide isomerase (PDI1-1) were followed at transcript level during grain development for three independent growth cycles to establish whether differences between cultivars were reproducible. Quantitative determination of PDI1-1 protein levels by ELISA confirmed a reproducibly, distinctive accumulation and post-translational modifications between cultivars, which were independent of plant growth regimes. According to its impact on differential storage protein accumulation, we propose the PDI1-1 protein as potential biomarker for Mexican malting barley cultivars.

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Section: Resultssupporting

confidence: 90%

Section: Resultsmentioning

confidence: 99%