S. Meziani, I. Nadaud, B. Gaillard-Martinie, C. Chambon, M. Benali, G. Branlard
{"title":"小麦及三个小麦相关种成熟粒糊粉层的蛋白质组学分析","authors":"S. Meziani, I. Nadaud, B. Gaillard-Martinie, C. Chambon, M. Benali, G. Branlard","doi":"10.30952/ns.8.1.5","DOIUrl":null,"url":null,"abstract":"Background : A proteomics approach was used to reveal major protein differences in the aleurone layer (AL) of mature grain between four wheat species: T. aestivum and T. spelta (6X), T. durum (4X), and T. monococum (2X). \nMateriel and methods: In each species, one representative cultivar was used for total AL protein extraction. Two-dimensional electrophoresis of AL proteins revealed 1380, 1355, 1120 and 973 Coomassie stained spots, respectively. \nResult: A total of 334 spots showed quantitative or qualitative (presence/absence) differences between the four cultivars. T. aestivum and T. spelta had 90.9% and 92.6% of their AL proteome respectively, identical to the other species. Only 25 spots were significantly different between the two hexaploid cultivars. AL proteins encoded by the A genome were mainly expressed in polyploid species. Percentages of proteins encoded by A genome was 85%, in tetraploid species and 70% in the hexaploid spelt. Eighty for proteins are identified by mass spectrometry and data mining and were classified in five bbiological processes and (12) functional categories. \nConclusion: The major differences between species were particularly due to storage globulins (22, 11 and 1 of Glo-3, Glo-3B, Glo-3C, respectively), stress related proteins including antioxidant proteins like 1-Cys peroxiredoxin and manganese superoxide dismutase, defence proteins like xylanase, serpin3 and heat shock proteins.","PeriodicalId":31426,"journal":{"name":"Nutrition Sante","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2019-06-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"2","resultStr":"{\"title\":\"Proteomic analysis of mature kernel aleurone layer of Triticum spelta and three wheat related species\",\"authors\":\"S. Meziani, I. Nadaud, B. Gaillard-Martinie, C. Chambon, M. Benali, G. Branlard\",\"doi\":\"10.30952/ns.8.1.5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Background : A proteomics approach was used to reveal major protein differences in the aleurone layer (AL) of mature grain between four wheat species: T. aestivum and T. spelta (6X), T. durum (4X), and T. monococum (2X). \\nMateriel and methods: In each species, one representative cultivar was used for total AL protein extraction. Two-dimensional electrophoresis of AL proteins revealed 1380, 1355, 1120 and 973 Coomassie stained spots, respectively. \\nResult: A total of 334 spots showed quantitative or qualitative (presence/absence) differences between the four cultivars. T. aestivum and T. spelta had 90.9% and 92.6% of their AL proteome respectively, identical to the other species. Only 25 spots were significantly different between the two hexaploid cultivars. AL proteins encoded by the A genome were mainly expressed in polyploid species. Percentages of proteins encoded by A genome was 85%, in tetraploid species and 70% in the hexaploid spelt. Eighty for proteins are identified by mass spectrometry and data mining and were classified in five bbiological processes and (12) functional categories. \\nConclusion: The major differences between species were particularly due to storage globulins (22, 11 and 1 of Glo-3, Glo-3B, Glo-3C, respectively), stress related proteins including antioxidant proteins like 1-Cys peroxiredoxin and manganese superoxide dismutase, defence proteins like xylanase, serpin3 and heat shock proteins.\",\"PeriodicalId\":31426,\"journal\":{\"name\":\"Nutrition Sante\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-06-30\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"2\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nutrition Sante\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.30952/ns.8.1.5\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nutrition Sante","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.30952/ns.8.1.5","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Proteomic analysis of mature kernel aleurone layer of Triticum spelta and three wheat related species
Background : A proteomics approach was used to reveal major protein differences in the aleurone layer (AL) of mature grain between four wheat species: T. aestivum and T. spelta (6X), T. durum (4X), and T. monococum (2X).
Materiel and methods: In each species, one representative cultivar was used for total AL protein extraction. Two-dimensional electrophoresis of AL proteins revealed 1380, 1355, 1120 and 973 Coomassie stained spots, respectively.
Result: A total of 334 spots showed quantitative or qualitative (presence/absence) differences between the four cultivars. T. aestivum and T. spelta had 90.9% and 92.6% of their AL proteome respectively, identical to the other species. Only 25 spots were significantly different between the two hexaploid cultivars. AL proteins encoded by the A genome were mainly expressed in polyploid species. Percentages of proteins encoded by A genome was 85%, in tetraploid species and 70% in the hexaploid spelt. Eighty for proteins are identified by mass spectrometry and data mining and were classified in five bbiological processes and (12) functional categories.
Conclusion: The major differences between species were particularly due to storage globulins (22, 11 and 1 of Glo-3, Glo-3B, Glo-3C, respectively), stress related proteins including antioxidant proteins like 1-Cys peroxiredoxin and manganese superoxide dismutase, defence proteins like xylanase, serpin3 and heat shock proteins.