Cold-Specific Induction of a Dehydrin Gene Family Member in Barley

Zee, Karen van; Qian, Jin-yuan; Hayes, Patrick; Close, Timothy J.; Chen, T. H. H.

doi:10.1104/pp.108.3.1233

Cited by 59 publications

(37 citation statements)

References 26 publications

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“…Ihe same phenomenon probably occurs m barley, -^ * f since the major cold-induced dehydrin, dhnS, is closely related to we SI 20 and maps to chromosome In maize, two dehydrin genes, dhnl {rablT) and 6H (van Zee et al, 1995). Other studies have also Lipase (see below), have been identified to date established positive correlations between freezing (Close et al, 1989;Pla et al, 1989;Paek et al, tolerance and accumulation of various cereal de-unpublished).…”

Section: Association Of Maize Dehydrin Genes With Adaptivementioning

confidence: 83%

Dehydrins: genes, proteins, and associations with phenotypic traits

1997

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SUMMARYDehydrin proteins (late embryogenesis abundant (LEA) Dll family) are produced in a wide variety of plant species in response to environmental stimuli with a dehydrative component, including drought, low temperature, salinity, and developmental stages such as seed and pollen maturation. Despite their widespread occurrence and abundance in cells under dehydrative conditions, the biochemical role of dehydrins remains elusive. The subcellular location of dehydrins is consistent with a biochemical role as an intracellular stabilizer, possibly with surfactant characteristics, acting upon targets in both the nucleus and cytoplasm. In some species, dehydrin loci are located within quantitative trait loci (QTL) intervals for important phenotypic traits including winter hardiness in barley {Hordeum vulgare L.) and an thesis-silking interval in maize {Zea mays L.). Dehydrin loci tend to be multigenic and occur in clusters on more than one chromosome. Investigations are currently under way in our laboratory and others' to move beyond protein accumulation studies and correlations with QTL to uncover direct cause-and-efTect relationships between dehydrin {dhn) genes and phenotypes associated with physiological responses to stress.

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Section: Association Of Maize Dehydrin Genes With Adaptivementioning

confidence: 83%

Dehydrins: genes, proteins, and associations with phenotypic traits

1997

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“…These authors have underlined that the recurring physiological and genetic correlations constitute mounting evidence that dehydrin genes may be key genetic determinants of stress tolerance in a number of species, particularly freezing and drought-tolerance. The first example was for a QTL for winter-hardiness overlapping a cluster of dhn genes, including dhn1 on barley chromosome 5H associated with a cold-specific induction of a member of this dehydrin family (Pan et al 1994;Van Zee et al 1995). The emergence of a biochemical role of these proteins show that they could preserve structural integrity, particularly membrane integrity, by inhibiting the coagulation of macromolecules (Close 1996(Close , 1997.…”

Section: Which Genes Under the Rwc Variation?mentioning

confidence: 98%

QTL for relative water content in field-grown barley and their stability across Mediterranean environments

et al. 2003

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A quantitative genetics approach was developed to identify the genomic regions that control relative water content (RWC) in field-grown barley. The trait was previously demonstrated to be a relevant screening tool of drought-tolerance in cereals, as well as a good indicator of plant water-status. The trait was measured at the heading stage on flag leaves recorded from 167 recombinant inbred lines grown in several Mediterranean sites (Montpellier, France; Meknès, Morocco; Le Kef, Tunisia). The results obtained confirmed that several genomic regions are implicated in the total phenotypic variation of RWC. A total of nine chromosomal regions were identified. One region situated on the long arm of chromosome 6H contains the most-consistent QTL obtained in the present study. This region was previously identified as controlling RWC, as well as leaf osmotic potential under water stress and osmotic adjustment, from an experiment conducted in growth-chamber conditions with the same genetic background. The confirmation of the role of this region in the genetic control of water and turgor status underlined its interest for breeding purposes in the Mediterranean area. In addition, the presence of several dehydrin loci in the same chromosomal area reinforce its interest for genomics analyses to confirm, or not to confirm, the implication of these genes in the variation of RWC.

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“…LEA proteins also display diverse subcellular and tissue-specific localization patterns, suggesting that different groups or group members fulfill specific functional roles (Close, 1997; Nylander et al., 2001). LEA protein expression generally correlates well with desiccation tolerance in young seedlings (Bartels et al, 1988; Reid and Walker-Simmons, 1993; Whisitt et al, 1997) as well as salt tolerance (Moons et al, 1995) and freezing tolerance (Houde et al, 1995;Van Zee et al, 1995; Close, 1997; Danyluk et al., 1998 Article, publication date, and citation information can be found at www.plantphysiol.org/cgi …”

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confidence: 99%

Temperature-Induced Extended Helix/Random Coil Transitions in a Group 1 Late Embryogenesis-Abundant Protein from Soybean

et al. 2002

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Group 1 late embryogenesis-abundant (LEA) proteins are a subset of hydrophilins that are postulated to play important roles in protecting plant macromolecules from damage during freezing, desiccation, or osmotic stress. To better understand the putative functional roles of group 1 LEA proteins, we analyzed the structure of a group 1 LEA protein from soybean (Glycine max). Differential scanning calorimetry of the purified, recombinant protein demonstrated that the protein assumed a largely unstructured state in solution. In the presence of trifluoroethanol (50% [w/v]), the protein acquired a 30% ␣-helical content, indicating that the polypeptide is highly restricted to adopt ␣-helical structures. In the presence of sodium dodecyl sulfate (1% [w/v]), 8% of the polypeptide chain adopted an ␣-helical structure. However, incubation with phospholipids showed no effect on the protein structure. Ultraviolet absorption and circular dichroism spectroscopy revealed that the protein existed in equilibrium between two conformational states. Ultraviolet absorption spectroscopy studies also showed that the protein became more hydrated upon heating. Furthermore, circular dichroism spectral measurements indicated that a minimum of 14% of amino acid residues existed in a solvent-exposed, left-handed extended helical or poly (l-proline)-type (PII) conformation at 20°C with the remainder of the protein being unstructured. The content of PII-like structure increased as temperature was lowered. We hypothesize that by favoring the adoption of PII structure, instead of the formation of ␣-helical or ␤-sheet structures, group 1 LEA proteins retain a high content of surface area available for interaction with the solvent. This feature could constitute the basis of a potential role of LEA proteins in preventing freezing, desiccation, or osmotic stress damage.Late embryogenesis-abundant (LEA) proteins accumulate to high concentrations in plant embryos during the latter stages of seed development before desiccation (Baker et al., 1988;Dure et al., 1989;Hughes and Galau, 1989). LEA proteins also accumulate in vegetative tissues exposed to exogenous abscisic acid, as well as dehydration, osmotic, and lowtemperature stress (Chandler and Robertson, 1994;Ingram and Bartels, 1996; Bray, 1997; Close, 1996 Close, , 1997Thomashow, 1998; Nylander et al., 2001). More than seven different groups of LEA proteins have been described and categorized by virtue of similarities in their deduced amino acid sequences (Baker et al., 1988;Dure et al., 1989). The majority of LEA proteins are highly hydrophilic and display a preponderance (e.g. Ala, Gly, Glu, and Thr) or lack (e.g. Trp and Cys) of certain amino acid residues (Dure, 1993a(Dure, , 1993b(Dure, , 1997. Thus, LEA proteins are part of a larger, evolutionarily conserved group of hydrophilic proteins termed "hydrophilins" involved in various adaptive responses to hyperosmotic conditions (Garay-Arroyo et al., 2000).Various functions have been proposed for different groups of LEA proteins ranging from wa...

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Cold-Specific Induction of a Dehydrin Gene Family Member in Barley

Cited by 59 publications

References 26 publications

Dehydrins: genes, proteins, and associations with phenotypic traits

Dehydrins: genes, proteins, and associations with phenotypic traits

QTL for relative water content in field-grown barley and their stability across Mediterranean environments

Temperature-Induced Extended Helix/Random Coil Transitions in a Group 1 Late Embryogenesis-Abundant Protein from Soybean

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