The role of dehydrins in plant response to cold

Kosová, Klára; Vítámvás, Pavel; Prášil, Ilja Tom

doi:10.1007/s10535-007-0133-6

Cited by 193 publications

(145 citation statements)

References 119 publications

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“…To lessen the negative effects of these environmental stresses, most, if not all, plants express dehydration proteins (dehydrins; Close, 1997;Allagulova et al, 2003;Rorat, 2006;Kosová et al, 2007;, a member of the group 2 LEA proteins. Dehydrins are thought to be involved in dehydration protection, since their transcription and translation are increased during dehydration, and a correlation exists between drought tolerance and the amount of dehydrin present.…”

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confidence: 99%

The Importance of Size and Disorder in the Cryoprotective Effects of Dehydrins

et al. 2013

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Dehydrins protect plant proteins and membranes from damage during drought and cold. Vitis riparia K 2 is a 48-residue protein that can protect lactate dehydrogenase from freeze-thaw damage by preventing the aggregation and denaturation of the enzyme. To further elucidate its mechanism, we used a series of V. riparia K 2 concatemers (K 4 , K 6 , K 8 , and K 10 ) and natural dehydrins (V. riparia YSK 2 , 60 kilodalton peach dehydrin [PCA60], barley dehydrin5 [Dhn5], Thellungiella salsuginea dehydrin2 , and Opuntia streptacantha dehydrin1 ) to test the effect of the number of K-segments and dehydrin size on their ability to protect lactate dehydrogenase from freeze-thaw damage. The results show that the larger the hydrodynamic radius of the dehydrin, the more effective the cryoprotection. A similar trend is observed with polyethylene glycol, which would suggest that the protection is simply a nonspecific volume exclusion effect that can be manifested by any protein. However, structured proteins of a similar range of sizes did not show the same pattern and level of cryoprotection. Our results suggest that with respect to enzyme protection, dehydrins function primarily as molecular shields and that their intrinsic disorder is required for them to be an effective cryoprotectant. Lastly, we show that the cryoprotection by a dehydrin is not due to any antifreeze proteinlike activity, as has been reported previously.

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The Importance of Size and Disorder in the Cryoprotective Effects of Dehydrins

et al. 2013

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“…The S-motif, a phosphorylatable serine tract containing five to eight residues, participates in nuclear targeting of the dehydrins (Close 1997). The K segment is a conserved lysine-rich, 15-amino-acid sequence (EKK-GIMDKIKEKLPG) that is found in all dehydrin genes, generally near the C-terminal region (Kosová et al 2007). There may be one or several copies of this region (Rorat et al 2006) which act as an interface between hydrophobic membrane phospholipids and the hydrophilic cytosol in plant cells, forming an amphipathic helix (Close 1997;Campbell and Close 1997;Hara et al 2009).…”

Section: Communicated By S González-martínezmentioning

confidence: 99%

Dehydrins in maritime pine (Pinus pinaster) and their expression related to drought stress response

Velasco-Conde

Yakovlev²,

Majada

et al. 2012

Tree Genetics & Genomes

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Maritime pine (Pinus pinaster) is an important commercial species throughout its Atlantic distribution. With the anticipated increase in desiccation of its habitat as a result of climate change, the selection of genotypes with increased survival and growth capability under these conditions for breeding programs is of great interest for this species. We aimed to study the response to a realistic drought stress under controlled conditions, looked for a method to measure dehydration resistance, and analyzed dehydrin expression in drought-resistant and drought-sensitive clones from different ecotypes. We report here the sequence characteristics and the expression patterns of five dehydrins from P. pinaster, along with the physiological characterization of drought stress responses in different genotypes (clonally replicated plants), originating from a broad geographical distribution across France and Spain (provenances). In total, we distinguished five different dehydrin genes in silico, grouped into two types-K 2 and SK n . Three of the dehydrin genes had several sequence variants, differing by multiple or single amino acid substitutions. Only two of the dehydrins (PpinDhn3 and PpinDhn4) showed an increase in transcription with increased drought stress which was dependent on provenance and genotype, suggesting their involvement in drought resistance. The other dehydrins showed decreased expression trends with increased severity of the drought stress. The lack of close association between the drought stress and expression patterns of these dehydrin genes suggest that they could have other functions and not be involved in drought resistance. Our results suggest large differences in function between different dehydrin genes.

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“…5). The discrepancy could be due to their high affinities to SDS, which is often found in LEA proteins with skewed amino acid compositions (Kosová et al, 2007, Battaglia et al, 2008 . Southern blot analyses of Ccor1/Ccor2 and homologous sequences in two strains of C. vulgaris.…”

Section: Heat Stability and Cryoprotectant Activities Of Ccor1 And Ccor2mentioning

confidence: 99%

“…LEA proteins can be induced in response to water deficit (Ingram and Bartels, 1996;Abba' et al, 2006) or cold (Hara et al, 2001;Kosová et al, 2007). Reyes et al (2005; suggested that LEA proteins can protect enzymes against the effects of water limitation and freeze-inactivation.…”

Section: Introductionmentioning

confidence: 99%