ArticleMolecular genetics and genomics : MGG2016
The starch-bound alpha-amylase/trypsin-inhibitors in Avena.
Article in Molecular genetics and genomics : MGG, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 13 citations in OpenAlex.
- Integrative lipidomics and proteomics reveal the aging mechanisms of heat-treated oat flour during long-term storage.Food chemistry: X · 2025Article
- Analysis of oat seed transcriptome with regards to proteins involved in celiac disease.Scientific reports · 2022Article
- Structure, Function and Protein Engineering of Cereal-Type Inhibitors Acting on Amylolytic Enzymes.Frontiers in molecular biosciences · 2022Review
- Wheat ATIs: Characteristics and Role in Human Disease.Frontiers in nutrition · 2021Review
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9 authors at 4 institutions in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Oat kernels exhibit an extra-soft texture, a trait recently demonstrated to be largely modulated by starch-bound tryptophan-rich 2S proteins, the vromindolines. In this study, fractionation by two-dimensional electrophoresis of starch-bound proteins in 25 oat (Avena sativa) cultivars and 11 diploid or tetraploid Avena species revealed novel 2S proteins called Avena α-amylase/trypsin-inhibitors (AATI) because of their sequence similarity with wheat α-amylase/trypsin inhibitors. Thirty-seven AATI polypeptides, about 14 kDa in size, were split into three families named AATI-1, AATI-2, and AATI-3 with different primary structures and isoelectric points. AATI-1 and AATI-2 proteins showed 55.5-60.0 % sequence similarity with wheat α-amylase inhibitors CM1, CM2, and CM16, which have been found to cause innate immunity responses in celiac disease and non-celiac gluten sensitivity. Diploid A-genome and tetraploid AC-genome oat species possess three and five genes encoding for the AATI proteins, respectively, whereas hexaploid A. sativa exhibits 12 genes dispersed over the A-, C-, and D-genomes. Some AATI proteins expressed in hexaploid oats were assigned to the A-genome based on similarity to their counterparts in diploid species, contributing to further clarify the genetic origin of hexaploid oats. Moreover, AATI may interact with starch-bound vromindolines in determining the extra-soft texture of oat kernels and, due to their balanced amino acid compositions, may contribute to the biological value of oat proteins in a positive manner.
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