at physiological pH Lti30 forms nanoscale aggregates when proximal to the membrane suggesting that Lti30 may protect the cell by "cross-linking" the membrane lipids.
Nuclear magnetic resonance analysis suggests that negatively charged lipid head groups electrostatically capture the protein's disordered K segments which locally fold up into alpha-helical segments on the membrane surface. Thus Lti30 conforms to the general theme of structure-function relationships by folding upon binding in spite of its disordered atypically hydrophilic and repetitive sequence signatures.
Data identify three factors that regulate the lipid interaction of Lti30 in vitro: (1) a pH dependent His on/off switch (2) phosphorylation by protein kinase C and (3) reversal of membrane binding by proteolytic digest.
Multiple combinations of mutations in the promoter of the XERO2 dehydrin gene were used to identify elements involved in abscisic acid and cold induction.
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