Alt a 1 fromAlternariainteracts with PR5 thaumatin-like proteins
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چکیده
منابع مشابه
Several thaumatin-like proteins bind to beta-1,3-glucans.
Pathogenesis-related proteins from intercellular fluid washings of stressed barley (Hordeum vulgare L.) leaves were analyzed to determine their binding to various water-insoluble polysaccharides. Three proteins (19, 16, and 15 kD) bound specifically to several water-insoluble beta-1,3-glucans. Binding of the barley proteins to pachyman occurred quickly at 22 degreesC at pH 5.0, even in the pres...
متن کاملDifferential expression of thaumatin-like proteins in sorghum infested with greenbugs.
This study was designed to quantitatively analyze the expression of thaumatin-like protein (TLP) at the transcriptional level in different sorghum lines when they were infested with greenbugs. Three sorghum lines, Tx7000, PI550607, and PI550610, were used. RNAs were isolated from the different sorghum lines that were infested with greenbugs at different infestation times. The resultant mRNA was...
متن کاملStructure of Haze Forming Proteins in White Wines: Vitis vinifera Thaumatin-Like Proteins
Grape thaumatin-like proteins (TLPs) play roles in plant-pathogen interactions and can cause protein haze in white wine unless removed prior to bottling. Different isoforms of TLPs have different hazing potential and aggregation behavior. Here we present the elucidation of the molecular structures of three grape TLPs that display different hazing potential. The three TLPs have very similar stru...
متن کاملQuantification of chitinase and thaumatin-like proteins in grape juices and wines.
Chitinases and thaumatin-like proteins are important grape proteins as they have a great influence on wine quality. The quantification of these proteins in grape juices and wines, along with their purification, is therefore crucial to study their intrinsic characteristics and the exact role they play in wines. The main isoforms of these two proteins from Chardonnay grape juice were thus purifie...
متن کاملCharacterization of genes for novel thaumatin-like proteins in Cryptomeria japonica.
Thaumatin-like proteins (TLPs) are induced by a variety of phytopathogens in many plants and several TLPs are allergenic. Previously, we isolated three TLP-encoding cDNAs (Cry j 3.1, Cry j 3.2 and Cry j 3.3) from a cDNA library derived from the pollen of Cryptomeria japonica D. Don. Here, we describe three new TLP cDNAs (Cry j 3.4, Cry j 3.5 and Cry j 3.6). We compared the sequences, the geneti...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2014
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2014.02.044