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Promoter analysis and immunolocalisation show that puroindoline genes are exclusively expressed in starchy endosperm cells of wheat grain Inra
Wiley, P.R.; Tosi, P.; Evrard, A.; Lovegrove, A.; Jones, H.D.; Shewry, P.R..
The purolindolines are small cysteine-rich proteins which are present in the grain of wheat. They have a major impact on the utilisation of the grain as they are the major determinants of grain texture, which affects both milling and baking properties. Bread and durum wheats were transformed with constructs comprising the promoter regions of the Puroindoline a (Pina) and Puroindoline b (Pinb) genes fused to the uidA (GUS) reporter gene. Nine lines showing 3:1 segregation for the transgene and comprising all transgene/species combinations were selected for detailed analysis of transgene expression during grain development. This showed that transgene expression occurred only in the starchy endosperm cells and was not observed in any other seed or vegetative...
Tipo: Journal Article Palavras-chave: PUROINDOLINE; GRAIN DE BLE GRAIN TEXTURE; LOCATION; PUROINDOLINES; TRANSGENIC WHEAT.
Ano: 2007 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD200946eaab70&uri=/notices/prodinra1/2010/08/
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Puroindoline-a and puroindoline-b interact with the Saccharomyces cerevisiae plasma membrane through different amino acids present in their tryptophan-rich domain Inra
Evrard, A.; Lagarde, V.; Joudrier, P.; Gautier, M.F..
Puroindolines are two small, basic cysteine-rich proteins isolated from Triticum aestivum seeds and characterized by a tryptophan-rich domain. They form the molecular basis of wheat grain hardness and display antimicrobial activity that may contribute to plant defence. Their antimicrobial activity is presumed to be due to their hydrophobic tryptophan-rich domain. However, little is known about their mode of action and there is no in vivo evidence that the binding of puroindolines to membranes is mediated by their tryptophan-rich domain. In this study, using a yeast complementation assay, we showed that puroindolines interact with the Saccharomyces cerevisiae plasma membrane. By site-directed mutagenesis of their tryptophan-rich domain, we determined that...
Tipo: Journal Article Palavras-chave: SACCHAROMYCES CEREVISIAE.
Ano: 2008 URL: http://www.prodinra.inra.fr/prodinra/pinra/doc.xsp?id=PROD20093e8d01c9&uri=/notices/prodinra1/2009/03/
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