Abstract
Celiac disease is the most common food-induced enteropathy in humans, with a prevalence of approximately 1% worldwide. It is induced by digestion-resistant, proline- and glutamine-rich seed storage proteins, collectively referred to as gluten, found in wheat (Triticum aestivum). Related prolamins are present in barley (Hordeum vulgare) and rye (Secale cereale). The incidence of both celiac disease and a related condition called nonceliac gluten sensitivity is increasing. This has prompted efforts to identify methods of lowering gluten in wheat, one of the most important cereal crops. Here, we used bulked segregant RNA sequencing and map-based cloning to identify the genetic lesion underlying a recessive, low-prolamin mutation (lys3a) in diploid barley. We confirmed the mutant identity by complementing the lys3a mutant with a transgenic copy of the wild-type barley gene and then used targeting-induced local lesions in genomes to identify induced single-nucleotide polymorphisms in the three homeologs of the corresponding wheat gene. Combining inactivating mutations in the three subgenomes of hexaploid bread wheat in a single wheat line lowered gliadin and low-molecular-weight glutenin accumulation by 50% to 60% and increased free and protein-bound lysine by 33%.
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Claims 5
Claim · model-written summary
The low-prolamin lys3a mutation in barley was traced to a genetic lesion.
- Taxon
- barley
.jpg?width=60)
Hordeum vulgaree0 - Gene
- lys3ae0
- Outcome
- genetic lesion underlying a recessive, low-prolamin mutatione0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
.jpg?width=500)
Verbatim
e0“identify the genetic lesion underlying a recessive, low-prolamin mutation (lys3a) in diploid barley”
Claim · model-written summary
A wild-type barley gene complemented the lys3a mutant, confirming its identity.
- Taxon
- barleyHordeum vulgaree0
- Treatment
- complementing the lys3a mutant with a transgenic copy of the wild-type barley genee0
- Gene
- lys3ae0
- Outcome
- confirmed the mutant identitye0
Not reportedComparatorDirection
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“confirmed the mutant identity by complementing the lys3a mutant with a transgenic copy of the wild-type barley gene”
Claim · model-written summary
Induced single-nucleotide polymorphisms were identified in all three wheat homeologs.
- Taxon
- wheat
Triticum aestivume0 - Gene
- corresponding wheat genee0
- Outcome
- induced single-nucleotide polymorphisms in the three homeologse0
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“identify induced single-nucleotide polymorphisms in the three homeologs of the corresponding wheat gene”
Claim · model-written summary
Combining inactivating mutations in all three bread wheat subgenomes lowered gliadin and low-molecular-weight glutenin accumulation by 50% to 60%.
- Taxon
- bread wheatTriticum aestivume0
- Treatment
- Combining inactivating mutations in the three subgenomese0
- Outcome
- gliadin and low-molecular-weight glutenin accumulatione0
- Direction
- lowerede0
- Value
- 50% to 60%e0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Combining inactivating mutations in the three subgenomes of hexaploid bread wheat in a single wheat line lowered gliadin and low-molecular-weight glutenin accumulation by 50% to 60%”
Claim · model-written summary
Combining inactivating mutations in bread wheat increased free and protein-bound lysine by 33%.
- Taxon
- bread wheatTriticum aestivume0
- Treatment
- Combining inactivating mutations in the three subgenomese0
- Outcome
- free and protein-bound lysinee0
- Direction
- increasede0
- Value
- 33%e0
Not reportedComparator
Organisms pictured · Representative pictures of the matched species, not figures from the paper.
Verbatim
e0“Combining inactivating mutations in the three subgenomes of hexaploid bread wheat in a single wheat line lowered gliadin and low-molecular-weight glutenin accumulation by 50% to 60% and increased free and protein-bound lysine by 33%”
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