Wheat and barley dehydrins under cold, drought, and salinity - what can LEA-II proteins tell us about plant stress response?
Status PubMed-not-MEDLINE Jazyk angličtina Země Švýcarsko Médium electronic-ecollection
Typ dokumentu časopisecké články, přehledy
PubMed
25071816
PubMed Central
PMC4089117
DOI
10.3389/fpls.2014.00343
Knihovny.cz E-zdroje
- Klíčová slova
- abiotic stress, barley, dehydrin dynamics, proteins, transcripts, wheat,
- Publikační typ
- časopisecké články MeSH
- přehledy MeSH
Dehydrins as a group of late embryogenesis abundant II proteins represent important dehydration-inducible proteins whose accumulation is induced by developmental processes (embryo maturation) as well as by several abiotic stress factors (low temperatures, drought, salinity). In the review, an overview of studies aimed at investigation of dehydrin accumulation patterns at transcript and protein levels as well as their possible functions in common wheat (Triticum aestivum), durum wheat (T. durum), and barley (Hordeum vulgare) plants exposed to various abiotic stress factors (cold, frost, drought, salinity) is provided. Possible roles of dehydrin proteins in an acquisition and maintenance of an enhanced frost tolerance are analyzed in the context of plant developmental processes (vernalization). Quantitative and qualitative differences as well as post-translational modifications in accumulated dehydrin proteins between barley cultivars revealing differential tolerance to drought and salinity are also discussed. Current knowledge on dehydrin role in wheat and barley response to major dehydrative stresses is summarized and the major challenges in dehydrin research are outlined.
Zobrazit více v PubMed
Battaglia M., Olvera-Carillo Y., Garciarrubio A., Campos F., Covarrubias A. A. (2008). The enigmatic LEA proteins and other hydrophilins. PubMed DOI PMC
Bravo L. A., Close T. J., Corcuera L. J., Guy C. L. (1999). Characterization of an 80-kDa dehydrin-like protein in barley responsive to cold acclimation. DOI
Bravo L. A., Gallardo J., Navarrete A., Olave N., Martínez J., Alberdi M., et al. (2003). Cryoprotective activity of a cold-induced dehydrin purified from barley. DOI
Brini F., Hanin M., Lumbreras V., Irar S., Pagès M., Masmoudi K. (2007a). Functional characterisation of DHN-5 a dehydrin showing a differential phosphorylation pattern in two Tunisian durum wheat ( DOI
Brini F., Hanin M., Lumbreras V., Amara I., Khoudi H., Hassairi A., et al. (2007b). Overexpression of wheat dehydrin DHN-5 enhances tolerance to salt and osmotic stress in PubMed DOI
Brini F., Saibi W., Amara I., Gargouri A., Masmoudi K., Hanin M. (2010). Wheat dehydrin DHN-5 exerts a heat-protective effect on β-glucosidase and glucose oxidase activities. PubMed DOI
Brini F., Yamamoto A., Jlaiel L., Takeda S., Hobo T., Dinh H. Q., et al. (2011). Pleiotropic effects of the wheat dehydrin DHN-5 on stress responses in PubMed DOI
Choi D. W., Close T. J. (2000). A newly identified barley gene, Dhn12, encoding a YSK2 DHN, is located on chromosome 6H and has embryo-specific expression. DOI
Choi D. W., Zhu B., Close T. J. (1999). The barley ( DOI
Close T. J. (1997). Dehydrins: a commonalty in the response of plants to dehydration and low temperature. DOI
Close T. J., Meyer N. C., Radik J. (1995). Nucleotide sequence of a gene encoding a 58.5-kilodalton barley dehydrin that lacks a serine tract. PubMed DOI PMC
Colmer T. D., Flowers T. J., Munns R. (2006). Use of wild relatives to improve salt tolerance in wheat. PubMed DOI
Danyluk J., Houde M., Rassart É., Sarhan F. (1994). Differential expression of a gene encoding an acidic dehydrin in chilling sensitive and freezing tolerant gramineae species. PubMed DOI
Danyluk J., Perron A., Houde M., Limin A., Fowler B., Benhamou N., et al. (1998). Accumulation of an acidic dehydrin in the vicinity of plasma membrane during cold acclimation of wheat. PubMed DOI PMC
Dhillon T., Pearce S. P., Stockinger E. J., Distelfeld A., Li C., Knox A. K., et al. (2010). Regulation of freezing tolerance and flowering in temperate cereals: the VRN-1 connection. PubMed DOI PMC
Drira M., Saibi W., Brini F., Gargouri A., Masmoudi K., 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. PubMed DOI
Ganeshan S., Vítámvás P., Fowler D. B., Chibbar R. N. (2008). Quantitative expression analysis of selected COR genes reveals their differential expression in leaf and crown tissues of wheat ( PubMed DOI PMC
Holková L., Mikulková P., Hrstková P., Prášil I. T., Bradáčová M., Prášilová P., et al. (2010). Allelic variations at Dhn4 and Dhn7 are associated with frost tolerance in barley.
Holková L., Prášil I. T., Bradáčová M., Vítámvás P., Chloupek O. (2009). Screening for frost tolerance in wheat using the expression of dehydrin genes Wcs120 and Wdhn13 at 17 DOI
Houde M., Dallaire S., N’Dong D., Sarhan F. (2004). Overexpression of the acidic dehydrin WCOR410 improves freezing tolerance in transgenic strawberry leaves. PubMed DOI
Houde M., Daniel C., Lachapelle M., Allard F., Laliberté S., Sarhan F. (1995). Immunolocalization of freezing-tolerance-associated proteins in the cytoplasm and nucleoplasm of wheat crown tissues. PubMed DOI
Houde M., Danyluk J., Laliberté J. F., Rassart E., Dhindsa R. S., Sarhan F. (1992). Cloning, characterization, and an expression of a cDNA encoding a 50-kilodalton protein specifically induced by cold acclimation in wheat. PubMed DOI PMC
Iturriaga G., Schneider K., Salamini F., Bartels D. (1992). Expression od desiccation-related proteins from the resurrection plant Craterostigma plantagineum in transgenic tobacco. PubMed DOI
Karami A., Shahbazi M., Niknam V., Shobbar Z. S., Tafreshi R. S., Abedini R., et al. (2013). Expression analysis of dehydrin multigene family across tolerant and susceptible barley ( DOI
Kosová K., Prášil I. T., Vítámvás P. (2008a). The relationship between vernalization- and photoperiodically-regulated genes and the development of frost tolerance in wheat and barley. DOI
Kosová K., Holková L., Prášil I. T., Prášilová P., Bradáčová M., Vítámvás P., et al. (2008b). Expression of dehydrin 5 during the development of frost tolerance in barley ( PubMed DOI
Kosová K., Prášil I. T., Vítámvás P. (2010). “Role of dehydrins in plant stress response,” in
Kosová K., Vítámvás P., Vlasáková E., Prášil I. T. (2013a). “The response of barley (
Kosová K., Vítámvás P., Prášilová P., Prášil I. T. (2013b). Accumulation of WCS120 and DHN5 proteins in differently frost-tolerant wheat and barley cultivars grown under a broad temperature scale. DOI
Ohno R., Takumi S., Nakamura C. (2003). Kinetics of transcript and protein accumulation of a low-molecular-weight wheat LEA-D11 dehydrin in response to low temperature. PubMed DOI
Prášil I.T., Holková L., Kosová K., Vítámvás P., Urban M. O., Musilová J., et al. (2014). “Quantitative expression of cold-regulated genes – a diagnostic marker for determination of frost tolerance in wheat,” in
Rodriguez E. M., Svensson J. T., Malatrasi M., Choi D. W., Close T. J. (2005). Barley Dhn13 encodes a KS-type dehydrin with constitutive and stress responsive expression. PubMed DOI
Rorat T. (2006). Plant dehydrins – tissue location, structure and function. PubMed DOI PMC
Sarhan F., Ouellet F., Vazquez-Tello A. (1997). The wheat Wcs120 gene family. A useful model to understand the genetics of freezing tolerance in cereals. DOI
Seo E., Lee H., Jeon J., Park H., Kim J., Noh Y. S., et al. (2009). Crosstalk between cold response and flowering in PubMed DOI PMC
Shitsukawa N., Ikari C., Mitsuya T., Sakiyama T., Ishikawa A., Takumi S., et al. (2007). Wheat SOC1 functions independently of WAP1/VRN1, an integrator of vernalization and photoperiod flowering promotion pathways. DOI
Škodáček Z., Prášil I. T. (2011). New possibilities for research of barley (
Sun X., Xi D. H., Feng H., Du J. B., Lei T., Liang H. G., et al. (2009). The dual effects of salicylic acid on dehydrin accumulation in water-stressed barley seedlings. DOI
Suprunova T., Krugman T., Fahima T., Chen G., Shams I., Korol A., et al. (2004). Differential expression of dehydrin genes in wild barley, DOI
The International Barley Genome Sequencing Consortium. (2012). A physical, genetic and functional sequence assembly of the barley genome. PubMed DOI
Tommasini L., Svensson J. T., Rodriguez E. M., Wahid A., Malatrasi M., Kato K., et al. (2008). Dehydrin gene expression provides an indicator of low temperature and drought stress: transcriptome-based analysis of barley ( PubMed DOI
Vítámvás P., Kosová K., Prášilová P., Prášil I. T. (2010). Accumulation of WCS120 protein in wheat cultivars grown at 9 DOI
Vítámvás P., Prášil I. T. (2008). WCS120 protein family and frost tolerance during cold acclimation, deacclimation and reacclimation of winter wheat. PubMed DOI
Vítámvás P., Saalbach G., Prášil I. T., Čapková V., Opatrná J., Jahoor A. (2007). WCS120 protein family and proteins soluble upon boiling in cold-acclimated winter wheat. PubMed DOI
Wang Y., Xu H., Zhu H., Tao Y., Zhang G., Zhang L., et al. (2014). Classification and expression diversification of wheat dehydrin genes. PubMed DOI
Wisniewski M., Webb R., Balsamo R., Close T. J., Yu X. M., Griffith M. (1999). Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: a dehydrin from peach ( DOI
Zhu B., Choi D. W., Fenton R., Close T. J. (2000). Expression of the barley dehydrin multigene family and the development of freezing tolerance. PubMed DOI
Zhu W., Zhang D., Lu X., Zhang L., Yu Z., Lv H., et al. (2014). Characterisation of an SKn-type dehydrin promoter from wheat and its responsiveness to various abiotic and biotic stresses. DOI
Light Quality and Intensity Modulate Cold Acclimation in Arabidopsis