30 research outputs found

    Kafirin structure and functionality

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    The structural and functional properties of kafirins are reviewed. Three classes of kafirin: the a, ß and ? forms have been identified at the protein level and one, the d, has been identified only at the gene and transcript levels. All forms show high homology with the equivalent zein proteins. By analogy with the zeins it is believed that the a-kafirins probably have an extended hairpin structure in solution, comprising elements of a-helix, ß-sheet and turns folded back on itself. Kafirins are the most hydrophobic of the prolamins as shown by their solubility, and calculated hydration free energies. The proteins exhibit extensive cross-linking by disulphide bonds and on cooking form indigestible aggregates which are not solubilised by reduction of disulphide bonds. In spite of continuing studies, the reasons for the low digestibility of the protein remain uncertain and there may be several factors involved. Other research has shown that kafirins may have non-food uses and may be used to form films

    The biochemistry and molecular biology of seed storage proteins

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    Asparagine In Plants

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    Interest in plant asparagine has rapidly taken off over the past 5 years following the report that acrylamide, a neurotoxin and potential carcinogen, is present in cooked foods, particularly carbohydrate-rich foods such as wheat and potatoes which are subjected to roasting, baking or frying at high temperatures. Subsequent studies showed that acrylamide could be formed in foods by the thermal degradation of free asparagine in the presence of sugars in the Maillard reaction. In this article, our current knowledge of asparagine in plants and in particular its occurrence in cereal seeds and potatoes is reviewed and discussed in relation to acrylamide formation. There is now clear evidence that soluble asparagine accumulates in most if not all plant organs during periods of low rates of protein synthesis and a plentiful supply of reduced nitrogen. The accumulation of asparagine occurs during normal physiological processes such as seed germination and nitrogen transport. 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    SnRK2 Protein Kinases—Key Regulators of Plant Response to Abiotic Stresses

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    The SnRK2 family members are plant-specific serine/threonine kinases involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. SnRK2s have been classed into three groups; group 1 comprises kinases not activated by ABA, group 2 comprises kinases not activated or activated very weakly by ABA, and group 3 comprises kinases strongly activated by ABA. So far, the ABA-dependent kinases belonging to group 3 have been studied most thoroughly. They are considered major regulators of plant response to ABA. The regulation of the plant response to ABA via SnRK2s pathways occurs by direct phosphorylation of various downstream targets, for example, SLAC1, KAT1, AtRbohF, and transcription factors required for the expression of numerous stress response genes. Members of group 2 share some cellular functions with group 3 kinases; however, their contribution to ABA-related responses is not clear. There are strong indications that they are positive regulators of plant responses to water deficit. Most probably they complement the ABA-dependent kinases in plant defense against environmental stress. So far, data concerning the physiological role of ABA-independent SnRK2s are very limited; it is to be expected they will be studied extensively in the nearest future

    A novel higher plant protein tyrosine phosphatase interacts with SNF1-related protein kinases via a KIS (kinase interaction sequence) domain

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    A novel protein phosphatase in Arabidopsis thaliana was identified by database searching. This protein, designated AtPTPKIS1, contains a protein tyrosine phosphatase (PTP) catalytic domain and a kinase interaction sequence (KIS) domain. It is predicted to interact with plant SNF1-related kinases (SnRKs), representing central regulators of metabolic and stress responses. AtPTPKIS1 has close homologues in other plant species, both dicots and monocots, but is not found in other kingdoms. The tomato homologue of AtPTPKIS1 was expressed as a recombinant protein and shown to hydrolyse a generic phosphatase substrate, and phosphotyrosine residues in synthetic peptides. The KIS domain of AtPTPKIS1 was shown to interact with the plant SnRK AKIN11 both in vivo in the yeast two-hybrid system, and in vitro in a GST-fusion 'pull down' assay. The genomes of Arabidopsis and other plants contain further predicted proteins related to AtPTPKIS1, which could also interact with SnRKs and act in novel regulatory and signalling pathways
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