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- W2005237935 abstract "The sequences of four oat cDNA clones, 3B3-5, 3B3-7, 3B3T-3 and 3B3T-5, isolated from developing seeds, are all found to possess sequences encoding a characteristic tryptophan-rich domain and, for this reason, have been named tryptophanins. 3B3-3 and 3B3-7 are predicted to encode two similar proteins, each consisting of 147 amino acids. 3B3T-3 and 3B3T-5 are predicted to encode identical proteins, 142 amino acids in length. The oat tryptophanins share sequence identity with two wheat seed proteins, puroindoline and wheat grain softness protein. The tryptophan-rich domains show similarity with the antimicrobial peptide, bovine indolicidin. Copy number reconstruction experiments indicate that the oat tryptophanins are encoded by a multi-gene family. RNA slot blot experiments verify the seed-specific expression of oat tryptophanins while northern blot experiments indicate that cross-hybridizing RNAs are also present in developing wheat, barley, and rye seeds but not in developing rice seeds." @default.
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- W2005237935 date "1998-10-01" @default.
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- W2005237935 title "Tryptophanins: isolation and molecular characterization of oat cDNA clones encoding proteins structurally related to puroindoline and wheat grain softness proteins" @default.
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