Proteomic analysis of endoplasmic reticulum stress responses in rice seeds

Qian, Dandan; Tian, Lihong; Qu, Le-Qing

doi:10.1038/srep14255

Cited by 46 publications

(30 citation statements)

References 55 publications

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“…The suppression or overexpression of BiP1 in rice endosperm led to ER stress, resulting in the change of expression patterns of starch synthesis-related genes and floury seeds (Wakasa et al, 2011). Moreover, proteomic analysis in ER-stressed rice seeds revealed changes in expression of carbohydrate metabolism-related proteins (Qian et al, 2015). Thus, the enhanced expression of ER chaperones such as OsBiP1 and OsPDIL1-1 in GPGb-RNAi transgenic rice seeds indicates that ER is an abnormal state, probably influencing carbohydrate metabolism.…”

Section: Discussionmentioning

confidence: 99%

RNA Interference-Mediated Simultaneous Suppression of Seed Storage Proteins in Rice Grains

Cho

Lee

et al. 2016

Front. Plant Sci.

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Seed storage proteins (SSPs) such as glutelin, prolamin, and globulin are abundant components in some of the most widely consumed food cereals in the world. Synthesized in the rough endoplasmic reticulum (ER), SSPs are translocated to the protein bodies. Prolamins are located at the spherical protein body I derived from the ER, whereas, glutelins and globulin are accumulated in the irregularly shaped protein bodies derived from vacuoles. Our previous studies have shown that the individual suppression of glutelins, 13-kDa prolamins and globulin caused the compensative accumulation of other SSPs. Herein, to investigate the phenotypic and molecular features of SSP deficiency transgenic rice plants suppressing all glutelins, prolamins, and globulin were generated using RNA interference (RNAi). The results revealed that glutelin A, cysteine-rich 13-kDa prolamin and globulin proteins were less accumulated but that glutelin B and ER chaperones, such as binding protein 1 (BiP1) and protein disulfide isomerase-like 1-1 (PDIL1-1), were highly accumulated at the transcript and protein levels in seeds of the transformants compared to those in the wild-type seeds. Further, the transcription of starch synthesis-related genes was reduced in immature seeds at 2 weeks after flowering, and the starch granules were loosely packaged with various sphere sizes in seed endosperms of the transformants, resulting in a floury phenotype. Interestingly, the rates of sprouting and reducing sugar accumulation during germination were found to be delayed in the transformants compared to the wild-type. In all, our results provide new insight into the role of SSPs in the formation of intracellular organelles and in germination.

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Section: Discussionmentioning

confidence: 99%

RNA Interference-Mediated Simultaneous Suppression of Seed Storage Proteins in Rice Grains

Cho

Lee

et al. 2016

Front. Plant Sci.

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“…The primary function of aminoacyl-tRNA synthetases is to couple tRNAs to corresponding amino acids participating in protein translation. The up-regulation of translatetion-related proteins such as tRNA synthetases has been observed in studies of endoplasmic reticulum stress responses in rice seeds (Qian et al 2015). Aminoacyl-tRNA synthetases have been found in marine alga and were up-regulated in response to Cu stress (Contreras et al 2010).…”

Section: Protein Involved In Translation and Synthesismentioning

confidence: 98%

Leaf proteome characterization in the context of physiological and morphological changes in response to copper stress in sorghum

et al. 2016

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Copper (Cu) is an essential micronutrient required for normal growth and development of plants; however, at elevated concentrations in soil, copper is also generally considered to be one of the most toxic metals to plant cells due to its inhibitory effects against many physiological and biochemical processes. In spite of its potential physiological and economical significance, molecular mechanisms under Cu stress has so far been grossly overlooked in sorghum. To explore the molecular alterations that occur in response to copper stress, the present study was performed in ten-day-old Cu-exposed leaves of sorghum seedlings. The growth characteristics were markedly inhibited, and ionic alterations were prominently observed in the leaves when the seedlings were exposed to different concentrations (0, 100, and 150 µM) of CuSO4. Using two-dimensional gels with silver staining, 643 differentially expressed protein spots (≥1.5-fold) were identified as either significantly increased or reduced in abundance. Of these spots, a total of 24 protein spots (≥1.5-fold) from Cu-exposed sorghum leaves were successfully analyzed by MALDI-TOF-TOF mass spectrometry. Of the 24 differentially expressed proteins from Cu-exposed sorghum leaves, 13 proteins were up-regulated, and 11 proteins were down-regulated. The abundance of most identified protein species, which function in carbohydrate metabolism, stress defense and protein translation, was significantly enhanced, while that of another protein species involved in energy metabolism, photosynthesis and growth and development were severely reduced. The resulting differences in protein expression patterns together with related morpho-physiological processes suggested that these results could help to elucidate plant adaptation to Cu stress and provide insights into the molecular mechanisms of Cu responses in C4 plants.

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“…The resin was subjected to 10% SDS-PAGE. The different bands were recovered, digested with trypsin, and subjected to MS analyses with the Triple TOF 5600 system (AB SCIEX) as described previously (Qian et al, 2015).…”

Section: Interaction Analysesmentioning

confidence: 99%

A β-Ketoacyl-CoA Synthase Is Involved in Rice Leaf Cuticular Wax Synthesis and Requires a CER2-LIKE Protein as a Cofactor

et al. 2016

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Cuticular waxes are complex mixtures of very-long-chain fatty acids (VLCFAs) and their derivatives, forming a natural barrier on aerial surfaces of terrestrial plants against biotic and abiotic stresses. In VLCFA biosynthesis, β-ketoacyl-CoA synthase (KCS) is the key enzyme, catalyzing the first reaction in fatty acid elongation and determining substrate specificity. We isolated a rice (Oryza sativa) wax crystal-sparse leaf 4 (WSL4) gene using a map-based cloning strategy. WSL4 is predicted to encode a KCS, a homolog of Arabidopsis (Arabidopsis thaliana) CER6. Complementation of the mutant wsl4-1 with WSL4 genomic DNA rescued the cuticular wax-deficient phenotype, confirming the function of WSL4 The load of wax components longer than 30 carbons (C30) and C28 were reduced markedly in wsl4-1 and wsl4-2 mutants, respectively. Overexpression of WSL4 increased the cuticular wax load in rice leaves. We further isolated a cofactor of WSL4, OsCER2, a homolog of Arabidopsis CER2, by coimmunoprecipitation and confirmed their physical interaction by split-ubiquitin yeast two-hybrid experiments. Expression of WSL4 alone in elo3 yeast cells resulted in increased C24 but did not produce VLCFAs of greater length, whereas expressing OsCER2 alone showed no effect. Coexpression of WSL4 and OsCER2 in elo3 yeast cells yielded fatty acids up to C30. OsCER2 with a mutated HxxxD motif (H172E, D176A, and D176H) interrupted its interaction with WSL4 and failed to elongate VLCFAs past C24 when expressed with WSL4 in elo3 yeast cells. These results demonstrated that WSL4 was involved in VLCFA elongation beyond C22 and that elongation beyond C24 required the participation of OsCER2.

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Proteomic analysis of endoplasmic reticulum stress responses in rice seeds

Cited by 46 publications

References 55 publications

RNA Interference-Mediated Simultaneous Suppression of Seed Storage Proteins in Rice Grains

RNA Interference-Mediated Simultaneous Suppression of Seed Storage Proteins in Rice Grains

Leaf proteome characterization in the context of physiological and morphological changes in response to copper stress in sorghum

A β-Ketoacyl-CoA Synthase Is Involved in Rice Leaf Cuticular Wax Synthesis and Requires a CER2-LIKE Protein as a Cofactor

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