Multifunctional roles of plant dehydrins in response to environmental stresses

Frontiers in Plant Science

Volumn 8, Issue , 2017, Pages

  Liu, Yang ^a   Song, Qiping ^a   Li, Daxing ^a   Yang, Xinghong ^a   Li, Dequan ^a  

^a SHANDONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

Abiotic stresses; Conserved segments; Dehydrin; Function; LEA protein

Indexed keywords

EID: 85021102101     PISSN: None     EISSN: 1664462X     Source Type: Journal    
DOI: 10.3389/fpls.2017.01018     Document Type: Review

References (40)

1. Alsheikh, M. K., Heyen, B. J., and Randall, S. K. (2003). Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation. J. Biol. Chem. 278, 40882-40889. doi: 10.1074/jbc.M307151200
2. Bao, F., Du, D., An, Y., Yang, W., Wang, J., Cheng, T., et al. (2017). Overexpression of Prunus mume dehydrin genes in tobacco enhances tolerance to cold and drought. Front. Plant Sci. 8:151. doi: 10.3389/fpls.2017.00151
3. Battaglia, M., Olvera-Carrillo, Y., Garciarrubio, A., Campos, F., and Covarrubias, A.A. (2008). The enigmatic LEA proteins and other hydrophilins. Plant Physiol. 148, 6-24. doi: 10.1104/pp.108.120725
4. Campbell, S. A., and Close, T. J. (1997). Dehydrins: genes, proteins, and associations with phenotypic traits. New Phytol. 137, 61-74. doi: 10.1046/j.1469-8137.1997.00831.x
5. Close, T. J. (1996). Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol. Plant. 97, 795-803. doi: 10.1111/j.1399-3054.1996.tb00546.x
6. Dean, R. T., Fu, S., Stocker, R., and Davies, M. J. (1997). Biochemistry and pathology of radical-mediated protein oxidation. Biochem. J. 324, 1-18. doi: 10.1042/bj3240001
7. Drira, M., Saibi, W., Amara, I., Masmoudi, K., Hanin, M., and Brini, F. (2015). Wheat dehydrin K-segments ensure bacterial stress tolerance, antiaggregation and antimicrobial effects. Appl. Biochem. Biotechnol. 175, 3310-3321. doi: 10.3389/fpls.2015.00406
8. Drira, M., Saibi, W., Brini, F., Gargouri, A., Masmoudi, K., and Hanin, M. (2013). The K-segments of the wheat dehydrin DHN-5 are essential for the protection of lactate dehydrogenase and β-glucosidase activities in vitro. Mol. Biotechnol. 54, 643-650. doi: 10.1007/s12033-012-9606-8
9. Dure, L., and Galau, G. A. (1981). Developmental biochemistry of cotton seed embryogenesis and germination XIII. Regulation of biosynthesis of principal storage proteins. Plant Physiol. 68, 187-194. doi: 10.1104/pp.68.1.187
10. Eriksson, S., Eremina, N., Barth, A., Danielsson, J., and Harryson, P. (2016). Membrane-induced folding of the plant-stress protein Lti30. Plant Physiol. 71, 932-943. doi: 10.1104/pp.15.01531
11. Eriksson, S. K., Kutzer, M., Procek, J., Grobner, G., and Harryson, P. (2011). Tunable membrane binding of the intrinsically disordered dehydrin Lti30, a cold-induced plant stress protein. Plant Cell 23, 2391-2404. doi: 10.1105/tpc.111.085183
12. Fan, N., Lv, A., Xie, J., Yuan, S., An, Y., and Zhou, P. (2017). Expression of CdDHN4, a novel YSK2-type dehydrin gene from bermudagrass, responses to drought stress through ABA-dependent signal pathway. Front. Plant Sci. 8:748. doi: 10.3389/fpls.2017.00748
13. Frank, W., Munnik, T., Kerkmann, K., Salamini, F., and Bartels, D. (2000). Water deficit triggers phospholipase D activity in the resurrection plant Craterostigma plantagineum. Plant Cell 12, 111-123. doi: 10.1105/tpc.12.1.111
14. Garay-Arroyo, A., Colmenero-Flores, J. M., Garciarrubio, A., and Covarrubias, A. A. (2000). Highly hydrophilic proteins in prokaryotes and eukaryotes are common during conditions of water deficit. J. Biol. Chem. 275, 5668-5674. doi: 10.1074/jbc.275.8.5668
15. Goday, A., Jensen, A. B., Culiàñez-Macià, F., Albà, M. M., Figueras, M., Serratosa, J., et al. (1994). The maize abscisic-acid responsive protein Rab17 is located in the nucleus and interacts with nuclear localization signals. Plant Cell 6, 351-360. doi: 10.1105/tpc.6.3.351
16. Hara, M., Fujinaga, M., and Kuboi, T. (2005). Metal binding by citrus dehydrin with histidine-rich domains. J. Exp. Bot. 56, 2695-2703. doi: 10.1093/jxb/eri262
17. Hara, M., Kondo, M., and Kato, T. (2013). A KS-type dehydrin and its related domains reduce Cu-promoted radical generation and the histidine residues contribute to the radical-reducing activities. J. Exp. Bot. 64, 1615-1624. doi: 10.1093/jxb/ert016
18. Hara, M., Monna, S., Murata, T., Nakano, T., Amano, S., Nachbar, M., et al. (2016). The Arabidopsis KS-type dehydrin recovers lactate dehydrogenase activity inhibited by copper with the contribution of his residues. Plant Sci. 245, 135-142. doi: 10.1016/j.plantsci.2016.02.006
19. Hara, M., Shinoda, Y., Kubo, M., Kashima, D., Takahashi, I., Kato, T., et al. (2011). Biochemical characterization of the Arabidopsis KS-type dehydrin protein, whose gene expression is constitutively abundant rather than stress dependent. Acta Physiol. Plant. 33, 2103-2116. doi: 10.1007/s11738-011-0749-1
20. Hara, M., Shinoda, Y., Tanaka, Y., and Kuboi, T. (2009). DNA binding of citrus dehydrin promoted by zinc ion. Plant Cell Environ. 32, 532-541. doi: 10.1111/j.1365-3040.2009.01947.x
21. Hara, M., Terashima, S., Fukaya, T., and Kuboi, T. (2003). Enhancement of cold tolerance and inhibition of lipid peroxidation by citrus dehydrin in transgenic tobacco. Planta 217, 290-298. doi: 10.1007/s00425-003-0986-7
22. Hara, M., Terashima, S., and Kuboi, T. (2001). Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu. J. Plant Physiol. 158, 1333-1339. doi: 10.1078/0176-1617-00600
23. Hughes, S. L., Schart, V., Malcolmson, J., Hogarth, K. A., Martynowicz, D. M., Tralman-Baker, E., et al. (2013). The importance of size and disorder in the cryoprotective effects of dehydrins. Plant Physiol. 163, 1376-1386. doi: 10.1104/pp.113.226803
24. Jensen, A. B., Goday, A., Figueras, M., Jessop, A. C., and Pages, M. (1998). Phosphorylation mediates the nuclear targeting of the maize Rab17 protein. Plant J. 13, 691-697. doi: 10.1046/j.1365-313X.1998.00069.x
25. Jiang, X., and Wang, Y. (2004). β-Elimination coupled with tandem mass spectrometry for the identification of in vivo and in vitro phosphorylation sites in maize dehydrin DHN1 protein. Biochemistry 43, 15567-15576. doi: 10.1021/bi0483965
26. Katagiri, T., Ishiyama, K., Kato, T., Tabata, S., Kobayashi, M., and Shinozaki, K. (2005). An important role of phosphatidic acid in ABA signaling during germination in Arabidopsis thaliana. Plant J. 43, 107-117. doi: 10.1111/j.1365-313X.2005.02431.x
27. Katagiri, T., Takahashi, S., and Shinozaki, K. (2001). Involvement of a novel Arabidopsis phospholipase D, AtPLDS, in dehydration-inducible accumulation of phosphatidic acid in stress signalling. Plant J. 26, 595-605. doi: 10.1046/j.1365-313x.2001.01060.x
28. Koag, M. C., Wilkens, S., Fenton, R. D., Resnik, J., Vo, E., and Close, T. J. (2009). The K-segment of maize DHN1 mediates binding to anionic phospholipid vesicles and concomitant structural changes. Plant Physiol. 150, 1503-1514. doi: 10.1104/pp.109.136697
29. Kooijman, E. E., Tieleman, D. P., Testerink, C., Munnik, T., Rijkers, D. T., Burger, K. N., et al. (2007). An electrostatic/hydrogen bond switch as the basis for the specific interaction of phosphatidic acid with proteins. J. Biol. Chem. 282, 11356-11364. doi: 10.1074/jbc.M609737200
30. Krüger, C., Berkowitz, O., Stephan, U. W., and Hell, R. (2002). A metalbinding member of the late embryogenesis abundant protein family transports iron in the phloem of Ricinus communis L. J. Biol. Chem. 277, 25062-25069. doi: 10.1074/jbc.M201896200
31. Lin, C. H., Peng, P. H., Ko, C. Y., Markhart, A. H., and Lin, T. Y. (2012). Characterization of a novel Y2K-type dehydrin VrDhn1 from Vigna radiata. Plant Cell Physiol. 53, 930-942. doi: 10.1093/pcp/pcs040
32. Liu, H., Yu, C., Li, H., Ouyang, B., Wang, T., Zhang, J., et al. (2015). Overexpression of ShDHN, a dehydrin gene from Solanum habrochaites enhances tolerance to multiple abiotic stresses in tomato. Plant Sci. 231, 198-211. doi: 10.1016/j.plantsci.2014.12.006
33. Liu, Y., Liang, J., Sun, L., Yang, X., and Li, D. (2016). Group 3 LEA protein, ZmLEA3, is involved in protection from low temperature stress. Front. Plant Sci. 7:1011. doi: 10.3389/fpls.2016.01011
34. Liu, Y., Wang, L., Xing, X., Sun, L., Pan, J., Kong, X., et al. (2013). ZmLEA3, a multifunctional group 3 LEA protein from maize (Zea mays L.), is involved in biotic and abiotic stresses. Plant Cell Physiol. 54, 944-959. doi: 10.1093/pcp/pct047
35. Malik, A. A., Veltri, M., Boddington, K. F., Singh, K. K., and Graether, S. P. (2017). Genome analysis of conserved dehydrin motifs in vascular plants. Front. Plant Sci. 8:709. doi: 10.3389/fpls.2017.00709
36. Mittler, R. (2002). Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci. 7, 405-410. doi: 10.1016/S1360-1385(02)02312-9
37. Petersen, J., Eriksson, S. K., Harryson, P., Pierog, S., Colby, T., Bartels, D., et al. (2012). The lysine-rich motif of intrinsically disordered stress protein CDeT11-24 from Craterostigma plantagineum is responsible for phosphatidic acid binding and protection of enzymes from damaging effects caused by desiccation. J. Exp. Bot. 63, 4919-4929. doi: 10.1093/jxb/ers173
38. Wise, M. J., and Tunnacliffe, A. (2004). POPP the question: what do LEA proteins do? Trends Plant Sci. 9, 13-17. doi: 10.1016/j.tplants.2003.10.012
39. Xie, C., Zhang, R. X., Qu, Y. T., Miao, Z. Y., Zhang, Y. Q., Shen, X. Y., et al. (2012). Overexpression of MtCAS31 enhances drought tolerance in transgenic Arabidopsis by reducing stomatal density. New Phytol. 195, 124-135. doi: 10.1111/j.1469-8137.2012.04136.x
40. Yang, W., Zhang, L., Lv, H., Li, H., Zhang, Y., Xu, Y., et al. (2015). The K-segments of wheat dehydrin WZY2 are essential for its protective functions under temperature stress. Front. Plant Sci. 6:406. doi:10.3389/fpls.2015.00406