The K-Segments of the Wheat Dehydrin DHN-5 are Essential for the Protection of Lactate Dehydrogenase and β-Glucosidase Activities In Vitro

Drira, M.; Saibi, Walid; Brini, Faïçal; Gargouri, Ali; Masmoudi, Khaled; Hanin, Moez

doi:10.1007/s12033-012-9606-8

Cited by 90 publications

(91 citation statements)

References 26 publications

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“…The presence of exogenous proline in culture medium reinforces this fact. Eventually and due to its multi-functionality, the ability to chelate salt and its molecular chaperone effect (Brini et al 2010;Drira et al 2013Drira et al , 2015, DHN-5 represents a real solution to minimize the negative effects of salt stress. Indeed, it is likely that it modulates mechanisms involved in salt tolerance, such as proline metabolism and ROS scavenging system.…”

Section: Proline Amount and Chlorophyll Level Account For Acquisitionmentioning

confidence: 99%

Durum wheat dehydrin (DHN-5) confers salinity tolerance to transgenic Arabidopsis plants through the regulation of proline metabolism and ROS scavenging system

Saibi

Feki

Mahmoud

et al. 2015

Planta

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The wheat dehydrin (DHN-5) gives birth to salinity tolerance to transgenic Arabidopsis plants by the regulation of proline metabolism and the ROS scavenging system. Dehydrins (DHNs) are involved in plant abiotic stress tolerance. In this study, we reported that salt tolerance of transgenic Arabidopsis plants overexpressing durum wheat dehydrin (DHN-5) was closely related to the activation of the proline metabolism enzyme (P5CS) and some antioxidant biocatalysts. Indeed, DHN-5 improved P5CS activity in the transgenic plants generating a significant proline accumulation. Moreover, salt tolerance of Arabidopsis transgenic plants was accompanied by an excellent activation of antioxidant enzymes like catalase (CAT), superoxide dismutase (SOD) and peroxide dismutase (POD) and generation of a lower level of hydrogen peroxide (H2O2) in leaves compared to the wild-type plants. The enzyme activities were enhanced in these transgenic plants in the presence of exogenous proline. Nevertheless, proline accumulation was slightly reduced in transgenic plants promoting chlorophyll levels. All these results suggest the crucial role of DHN-5 in response to salt stress through the activation of enzymes implicated in proline metabolism and in ROS scavenging enzymes.

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Section: Proline Amount and Chlorophyll Level Account For Acquisitionmentioning

confidence: 99%

Durum wheat dehydrin (DHN-5) confers salinity tolerance to transgenic Arabidopsis plants through the regulation of proline metabolism and ROS scavenging system

Saibi

Feki

Mahmoud

et al. 2015

Planta

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“…Based on these observations, the authors suggested that the K-segments must be important for the recovery of LDH activity. A recently published paper on wheat (Triticum aestivum) DHN-5, also using deletion mutants, suggested that the K-segments are critical for dehydrin's protective functions (Drira et al, 2013).…”

Section: Enzymatic Cryoprotectionmentioning

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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“…Less conserved motifs, the ø-segments are usually rich in polar amino acids and lay interspersed between K-segments [24] [51]. The K-segments of the wheat dehydrin DHN-5 are essential for the protection of lactate dehydrogenase and β-glucosidase activities in vitro [52]. The presence and arrangement of these different motifs in a single polypeptide allow the classification of group 2 LEA proteins into five subgroups [53] [54].…”

Section: Lea Groupmentioning

confidence: 99%

Insights into Late Embryogenesis Abundant (LEA) Proteins in Plants: From Structure to the Functions

Amara¹,

Zaïdi²,

Masmoudi³

et al. 2014

AJPS

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Late Embryogenesis Abundant (LEA) proteins, a group of hydrophilic proteins, have been linked to survival in plants and animals in periods of stress, putatively through safeguarding enzymatic function and prevention of aggregation in times of dehydration/heat. Yet despite decades of effort, the molecular-level mechanisms defining this protective function remain unknown. In this paper, we summarize and review research discoveries of the classification of the LEA protein groups based on their amino acid sequence similarity and on the presence of distinctive conserved motifs. Moreover, we focus on high correlation between their accumulation and water deficit, reinforcing their functional relevance under abiotic stresses. We also discuss the biochemical properties of LEA proteins arising from their hydrophilic nature and by amino acid composition. Although significant similarities have not been found between the members of the different groups, a unifying and outstanding feature of most of them is their high hydrophilicity and high content of glycine. Therefore, we have highlighted the biotechnological applications of LEA genes, and the effects of over-expressing LEA genes from all LEA groups from different species of origin into different plant hosts. Apart from agronomical purposes, LEA proteins could be useful for other biotechnological applications in relation to their capacity to prevent aggregation of proteins.

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The K-Segments of the Wheat Dehydrin DHN-5 are Essential for the Protection of Lactate Dehydrogenase and β-Glucosidase Activities In Vitro

Cited by 90 publications

References 26 publications

Durum wheat dehydrin (DHN-5) confers salinity tolerance to transgenic Arabidopsis plants through the regulation of proline metabolism and ROS scavenging system

Durum wheat dehydrin (DHN-5) confers salinity tolerance to transgenic Arabidopsis plants through the regulation of proline metabolism and ROS scavenging system

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

Insights into Late Embryogenesis Abundant (LEA) Proteins in Plants: From Structure to the Functions

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