Antifreeze proteins in overwintering plants: a tale of two activities

Griffith, Marilyn; Yaish, Mahmoud W.

doi:10.1016/j.tplants.2004.06.007

Cited by 475 publications

(377 citation statements)

References 48 publications

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“…We investigated the THFs in adult darkling beetles, U. ceramboides, from interior Alaska because they tolerate freezing to Ϫ60°C in midwinter (19) and were reported to exhibit Ϸ0.4°C of TH in their hemolymph after cold acclimation (9). We typically observed TH values Ͻ0.1°C and often detected only hexagonal ice crystal morphology in the hemolymph of cold-adapted insects, indicating the presence of a low concentration of THF and/or a low specific activity THF (6). The sporadic presence of Ͼ0.5°C of TH in the hemolymph of U. ceramboides is consistent with observations on other freezetolerant arthropods (16,20).…”

Section: Thf Isolated From U Ceramboides Is Highly Active and Contaimentioning

confidence: 99%

“…Although the physiological role of THFs in freeze-tolerance is not well understood, THFs do appear to promote cold tolerance. Recrystallization inhibition and/or TH activity are known to increase in response to low temperature in freeze-tolerant insects (16,17), other arthropods (20) and plants (6). For the centipede, Lithobius forficatus, experiments showed that THFs (i.e., AFPs) significantly increased cell survivorship under freez- ing conditions (29), although the mechanism remains unclear.…”

Section: Thf Contains a ␤-Mannopyranose-(134) ␤-Xylopyranose Backbonementioning

confidence: 99%

“…This body of work has revealed the existence of five distinct structural classes of fish AF(G)Ps (5) and has demonstrated some unexpected functions of these proteins. In addition to producing TH, all AF(G)Ps appear to prevent the recrystallization of ice (6), and certain fish AF(G)Ps may protect cell membranes from low-temperature-induced injury (7,8).…”

mentioning

confidence: 99%

“…Structurally distinct AF(G)Ps have been isolated and characterized from plants, insects, collembola, fungi, and bacteria (6,(12)(13)(14)(15), showing that diverse proteins with TH activity have evolved in distantly related cold-tolerant organisms. However, the majority of the responsible thermal hysteresis factors (THFs) have not been isolated or structurally characterized (i.e., chemical composition has not been determined).…”

mentioning

confidence: 99%

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A nonprotein thermal hysteresis-producing xylomannan antifreeze in the freeze-tolerant Alaskan beetle Upis ceramboides

Walters¹,

Serianni

Sformo

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

102

117

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Thermal hysteresis (TH), a difference between the melting and freezing points of a solution that is indicative of the presence of large-molecular-mass antifreezes (e.g., antifreeze proteins), has been described in animals, plants, bacteria, and fungi. Although all previously described TH-producing biomolecules are proteins, most thermal hysteresis factors (THFs) have not yet been structurally characterized, and none have been characterized from a freeze-tolerant animal. We isolated a highly active THF from the freeze-tolerant beetle, Upis ceramboides, by means of ice affinity. Amino acid chromatographic analysis, polyacrylamide gel electrophoresis, UV-Vis spectrophotometry, and NMR spectroscopy indicated that the THF contained little or no protein, yet it produced 3.7 ؎ 0.3°C of TH at 5 mg/ml, comparable to that of the most active insect antifreeze proteins. Compositional and structural analyses indicated that this antifreeze contains a ␤-mannopyranosyl-(134) ␤-xylopyranose backbone and a fatty acid component, although the lipid may not be covalently linked to the saccharide. Consistent with the proposed structure, treatment with endo-␤-(134)xylanase ablated TH activity. This xylomannan is the first TH-producing antifreeze isolated from a freeze-tolerant animal and the first in a new class of highly active THFs that contain little or no protein.antifreeze protein ͉ insect cold tolerance ͉ glycolipid ͉ membrane associated antifreeze

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Section: Thf Isolated From U Ceramboides Is Highly Active and Contaimentioning

confidence: 99%

Section: Thf Contains a ␤-Mannopyranose-(134) ␤-Xylopyranose Backbonementioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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A nonprotein thermal hysteresis-producing xylomannan antifreeze in the freeze-tolerant Alaskan beetle Upis ceramboides

Walters¹,

Serianni

Sformo

et al. 2009

Proc. Natl. Acad. Sci. U.S.A.

102

117

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“…The proteins are known as antifreeze proteins (AFPs) or antifreeze glycoproteins (AFGPs). 1 Thus far, these proteins have been found in various species of fish, 2-4 insects, [5][6][7] bacteria 8,9 and plants 10,11 (hereafter, AFPs and AFGPs are collectively referred to as AFPs).…”

Section: Introductionmentioning

confidence: 99%

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

Nada

Furukawa

2012

Polym J

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Antifreeze proteins (AFPs), which are present in the bodily fluids of organisms inhabiting cold environments, function as inhibitors of ice growth by binding to certain planes of ice crystals. However, the exact mechanism of ice growth inhibition is still poorly understood as it is exceedingly difficult to experimentally analyze the molecular-scale growth kinetics of ice crystals at the planes to which the proteins bind. This review paper focuses on computer simulation studies on the mechanism of ice growth inhibition by AFPs. Recent molecular dynamics simulations of a growing ice-water interface to which protein is bound have indicated that, when the protein is stably bound to the interface, the growth rate of ice surrounding the protein decreases drastically, owing to depression of the ice melting point through the Gibbs-Thomson effect. The observed decrease in growth rate is expected to correspond to ice growth inhibition in real-world systems. In addition to presenting published simulation studies on the mechanism of ice growth inhibition by AFPs, this review also outlines the direction of future simulation studies in this field.

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Cold Acclimation and Freezing Tolerance in Plants

Ouellet¹

2007

Encyclopedia of Life Sciences

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Antifreeze proteins in overwintering plants: a tale of two activities

Cited by 475 publications

References 48 publications

A nonprotein thermal hysteresis-producing xylomannan antifreeze in the freeze-tolerant Alaskan beetle Upis ceramboides

A nonprotein thermal hysteresis-producing xylomannan antifreeze in the freeze-tolerant Alaskan beetle Upis ceramboides

Antifreeze proteins: computer simulation studies on the mechanism of ice growth inhibition

Cold Acclimation and Freezing Tolerance in Plants

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