Purification of a Maize Dehydrin

Ceccardi, Toni L.; Meyer, Nicole C.; Close, T.J.

doi:10.1006/prep.1994.1040

Cited by 59 publications

(46 citation statements)

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“…However, WCOR410 proteins that accumulate during cold acclimation would be available to fulfill their cryoprotective function upon occurrence of freezing temperatures. In support of this concept, Ceccardi et al (1994) have shown that maize G50 dehydrin is capable of substantial hydrophobic interaction in vitro. This led Close (1996) to suggest that a possible function of the amphipathic ␣ helix within the K segment may be its hydrophobic interaction with partially denatured proteins or membranes.…”

Section: Discussionmentioning

confidence: 84%

Accumulation of an Acidic Dehydrin in the Vicinity of the Plasma Membrane during Cold Acclimation of Wheat

et al. 1998

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Expression of the acidic dehydrin gene wcor410 was found to be associated with the development of freezing tolerance in several Gramineae species. This gene is part of a family of three homologous members, wcor410 , wcor410b , and wcor410c , that have been mapped to the long arms of the homologous group 6 chromosomes of hexaploid wheat. To gain insight into the function of this gene family, antibodies were raised against the WCOR410 protein and affinity purified to eliminate cross-reactivity with the WCS120 dehydrin-like protein of wheat. Protein gel blot analyses showed that the accumulation of WCOR410 proteins correlates well with the capacity of each cultivar to cold acclimate and develop freezing tolerance. Immunoelectron microscope analyses revealed that these proteins accumulate in the vicinity of the plasma membrane of cells in the sensitive vascular transition area where freeze-induced dehydration is likely to be more severe. Biochemical fractionation experiments indicated that WCOR410 is a peripheral protein and not an integral membrane protein. These results provide direct evidence that a subtype of the dehydrin family accumulates near the plasma membrane. The properties, abundance, and localization of these proteins suggest that they are involved in the cryoprotection of the plasma membrane against freezing or dehydration stress. We propose that WCOR410 plays a role in preventing the destabilization of the plasma membrane that occurs during dehydrative conditions.

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Section: Discussionmentioning

confidence: 84%

Accumulation of an Acidic Dehydrin in the Vicinity of the Plasma Membrane during Cold Acclimation of Wheat

et al. 1998

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“…Could the dehydrins then act as water reservoirs that expel coordinated water to the surrounding medium (Boudet et al, 2006)? Considering the finding that the in vivo concentration of dehydrins does not seem to exceed 2% to 4% of cytoplasmic proteins, however, the benefit of such water expulsion is likely to be marginal (Roberts et al, 1993;Ceccardi et al, 1994;Close, 1996), at least in moderate drought. More likely, the molecular action of the dehydrins is more specific.…”

Section: Resultsmentioning

confidence: 99%

Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse

2008

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The dehydrins are a class of drought-induced proteins in plants that lack a fixed three-dimensional structure. Their specific molecular action, as well as the reason for their disordered character, is as yet poorly understood. It has been speculated, however, that the dehydrins are tuned to acquire a biologically active structure only under the conditions in which they normally function (i.e. upon dehydration). To test this hypothesis, we here investigate the effect of reduced water content and macromolecular crowding on three dehydrins from Arabidopsis (Arabidopsis thaliana). As a simplistic model for mimicking cellular dehydration, we used polyethylene glycol, glycerol, and sugars that plants naturally employ as compatible solutes (i.e. sucrose and glucose). Macromolecular crowding was induced by the large polysaccharides Ficoll and dextran. The results show that the dehydrins are remarkably stable in their disordered state and are only modestly affected by the solvent alterations. A notable exception is the dehydrin Cor47, which shows a small, intrinsic increase in helical structure at high concentrations of osmolytes. We also examined the effect of phosphorylation but found no evidence that such posttranslational modifications of the dehydrin sequences modulate their structural response to osmolytes and crowding agents. These results suggest that the dehydrins are highly specialized proteins that have evolved to maintain their disordered character under conditions in which unfolded states of several globular proteins would tend to collapse.

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“…Although their sequence is unrelated to that of Group 3 LEA proteins, the other main categories of LEA protein (i.e. Group 1 and Group 2, the latter frequently referred to as dehydrins) also seem to be wholly or partially natively unfolded (53)(54)(55)(56)(57)(58)(59)(60), suggesting that this is a general characteristic of LEA proteins.…”

Section: Discussionmentioning

confidence: 97%

Transition from Natively Unfolded to Folded State Induced by Desiccation in an Anhydrobiotic Nematode Protein

Goyal

Tisi

Basran

et al. 2003

Journal of Biological Chemistry

186

187

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Late embryogenesis abundant (LEA) proteins are associated with desiccation tolerance in resurrection plants and in plant seeds, and the recent discovery of a dehydration-induced Group 3 LEA-like gene in the nematode Aphelenchus avenae suggests a similar association in anhydrobiotic animals. Despite their importance, little is known about the structure of Group 3 LEA proteins, although computer modeling and secondary structure algorithms predict a largely ␣-helical monomer that forms coiled coil oligomers. We have therefore investigated the structure of the nematode protein, Aav-LEA1, in the first such analysis of a well characterized Group 3 LEA-like protein. Immunoblotting and subunit cross-linking experiments demonstrate limited oligomerization of AavLEA1, but analytical ultracentrifugation and gel filtration show that the vast majority of the protein is monomeric. Moreover, CD, fluorescence emission, and Fourier transform-infrared spectroscopy indicate an unstructured conformation for the nematode protein. Therefore, in solution, no evidence was found to support structure predictions; instead, Aav-LEA1 seems to be natively unfolded with a high degree of hydration and low compactness. Such proteins can, however, be induced to fold into more rigid structures by partner molecules or by altered physiological conditions. Because AavLEA1 is associated with desiccation stress, its Fourier transform-infrared spectrum in the dehydrated state was examined. A dramatic but reversible increase in ␣-helix and, possibly, coiled coil formation was observed on drying, indicating that computer predictions of secondary structure may be correct for the solid state. This unusual finding offers the possibility that structural shifts in Group 3 LEA proteins occur on dehydration, perhaps consistent with their role in anhydrobiosis.

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Purification of a Maize Dehydrin

Cited by 59 publications

References 0 publications

Accumulation of an Acidic Dehydrin in the Vicinity of the Plasma Membrane during Cold Acclimation of Wheat

Accumulation of an Acidic Dehydrin in the Vicinity of the Plasma Membrane during Cold Acclimation of Wheat

Mimicking the Plant Cell Interior under Water Stress by Macromolecular Crowding: Disordered Dehydrin Proteins Are Highly Resistant to Structural Collapse

Transition from Natively Unfolded to Folded State Induced by Desiccation in an Anhydrobiotic Nematode Protein

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