Tryptophanins: isolation and molecular characterization of oat cDNA clones encoding proteins structurally related to puroindoline and wheat grain softness proteins

Tanchak M.A., Schernthaner J.P., Giband Marc, Altosaar Illimar. 1998. Tryptophanins: isolation and molecular characterization of oat cDNA clones encoding proteins structurally related to puroindoline and wheat grain softness proteins. Plant Science, 137 : 173-184.

Résumé : 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.

Mots-clés Agrovoc : Avena, clone, adn, séquence nucléotidique, tryptophane, Triticum, albumine, endosperme, protéine de réserve

Classification Agris : F30 - Génétique et amélioration des plantes

Auteurs et affiliations

• Tanchak M.A.
• Schernthaner J.P.
• Giband Marc, CIRAD-CA-COTON (FRA) ORCID: 0000-0002-5553-5614
• Altosaar Illimar

Source : Cirad - Agritrop (https://agritrop.cirad.fr/390491/)

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