A single amino acid substitution in puroindoline b impacts its self-assembly and the formation of heteromeric assemblies with puroindoline a |
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| Affiliation: | 1. School of Agriculture, Food & Wine, The University of Adelaide, Glen Osmond, South Australia 5064, Australia;2. Australian Centre for Plant Functional Genomics, The University of Adelaide, Glen Osmond, South Australia 5064, Australia;1. Department of Agroecology, Aarhus University, Denmark;2. Department of Plant and Environmental Sciences, University of Copenhagen, Denmark;1. School of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China;2. Institute of Food Science and Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China;3. National Engineering Research Center for Functional Food, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China;4. State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi 214122, China |
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| Abstract: | ![]()
Puroindolines (PINs) A and B were purified from soft (Paledor) and hard (Recital, Courtot) wheat cultivars. Their purity and heterogeneity due to post-translational processing were characterized by SDS- and acid-PAGE, reversed-phase HPLC and mass spectrometry. By using dynamic light scattering (DLS), asymmetrical flow field-flow fractionation (AF4) and size exclusion chromatography (SEC), we showed that the size distributions of PINA are similar for the three varieties and that, in solution, they self-assembled into small aggregates, mainly dimers. Conversely, PINB isolated from hard varieties (PINB-D1b and PINB-D1d) are assembled into large aggregates while PINB-D1a formed small aggregates, mainly monomers. Mixed solutions of PINA and PINB formed heteromeric aggregates. The large PINB-D1b aggregates were retained even at a high (4:1) PINA/PINB weight ratio. Reversible dissociation of large aggregates into small aggregates suggested that weak interactions control the self-assembly of PINs. The aggregative properties of PINs have now to be taken into account when studying their interactions with other components to decipher the causal relationships between these proteins and grain hardness. |
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| Keywords: | Puroindolines Wheat hardness Self-assembly AF4" },{" #name" :" keyword" ," $" :{" id" :" kwrd0030" }," $$" :[{" #name" :" text" ," _" :" asymmetrical flow field-flow fractionation DLS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0040" }," $$" :[{" #name" :" text" ," _" :" dynamic light scattering HPLC" },{" #name" :" keyword" ," $" :{" id" :" kwrd0050" }," $$" :[{" #name" :" text" ," _" :" high performance liquid chromatography PAGE" },{" #name" :" keyword" ," $" :{" id" :" kwrd0060" }," $$" :[{" #name" :" text" ," _" :" polyacrylamide gel electrophoresis PINA" },{" #name" :" keyword" ," $" :{" id" :" kwrd0070" }," $$" :[{" #name" :" text" ," _" :" puroindoline a PINB" },{" #name" :" keyword" ," $" :{" id" :" kwrd0080" }," $$" :[{" #name" :" text" ," _" :" puroindoline b PINs" },{" #name" :" keyword" ," $" :{" id" :" kwrd0090" }," $$" :[{" #name" :" text" ," _" :" puroindoline a and puroindoline b SEC" },{" #name" :" keyword" ," $" :{" id" :" kwrd0100" }," $$" :[{" #name" :" text" ," _" :" size exclusion chromatography SDS" },{" #name" :" keyword" ," $" :{" id" :" kwrd0110" }," $$" :[{" #name" :" text" ," _" :" sodium dodecyl sulfate WT" },{" #name" :" keyword" ," $" :{" id" :" kwrd0120" }," $$" :[{" #name" :" text" ," _" :" wild type |
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