Desiccation tolerance in developing soybean seeds: The role of stress proteins

Blackman, Sheila A.; Obendorf, Ralph L.; Leopold, A. C.

doi:10.1111/j.1399-3054.1995.tb05110.x

Cited by 88 publications

(34 citation statements)

References 29 publications

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“…Proteome analysis confirmed that M. truncatula dehydrins are associated with desiccation tolerance (Boudet et al 2006). The LEA proteins are thought to participate in desiccation tolerance (Dure 1993;Close 1996;Han et al 1997;Kermode 1997) and their accumulation suggests that these proteins prevent or reduce desiccation-induced cellular damage (Blackman et al 1995). Dehydrins play a role in desiccation tolerance initiation in wheat (Triticum aestivum L.) classified as orthodox (Black et al 1999).…”

Section: Discussionmentioning

confidence: 89%

“…Electrolyte leakage illustrates the relationship between membrane integrity and stability and drying and desiccation tolerance (Sun and Leopold 1993). This method is commonly used to determine the acquisition of desiccation tolerance in developing seeds (Sun and Leopold 1993;Blackman et al 1995;Liang and Sun 2000;Pukacka and Ratajczak 2007a).…”

Section: Discussionmentioning

confidence: 99%

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Desiccation tolerance acquisition in developing beech (Fagus sylvatica L.) seeds: the contribution of dehydrin-like protein

Kalemba

Janowiak

Pukacka

2008

Trees

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The acquisition of desiccation tolerance (DT) in developing beech (Fagus sylvatica L.) seeds and the role of a dehydrin protein in this process were investigated. DT was determined by measurement of electrolyte leakage and germination capacity after drying to 10-12% moisture content (MC). In addition to mass maturity, the presence of heat-stable proteins, dehydrin accumulation and the peak of ABA content were measured in relation to the acquisition of DT. Mass maturity was achieved at 16 weeks after flowering (WAF). The germination capacity increased from 8% at 12 WAF to 80-90% after 16 WAF. Cell membrane integrity, measured as a decrease in electrolyte leakage after desiccation, was acquired at 16 WAF. Additionally, the ratio of heat-stable to soluble proteins was the highest at 16 WAF. One dehydrin-like protein with a molecular mass 44 kDa, named DHN44, was detected in embryonic axes at 16 WAF and in cotyledons at 17 WAF, and its gradual accumulation was observed in mature seeds. With regard to the acquisition of DT, the strongest correlations were detected between electrolyte leakage, DHN44 accumulation, and the percentage of heat-stable proteins. These results suggest that developing beech seeds become tolerant to desiccation at 16 WAF. The effect of desiccation and ABA treatment on DHN44 synthesis was tested before (14 WAF) and after the DT acquisition (18 WAF).Depending on the maturation stage desiccation and ABA treatment can induce or enlarge DHN44 expression.

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Section: Discussionmentioning

confidence: 89%

Section: Discussionmentioning

confidence: 99%

Desiccation tolerance acquisition in developing beech (Fagus sylvatica L.) seeds: the contribution of dehydrin-like protein

Kalemba

Janowiak

Pukacka

2008

Trees

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“…Response to desiccation stress, salt stress and cold stress have also been noted (see discussion in Bray 2000 andWise 2003), and improved stress tolerance often correlates with LEA protein expression. For example, Blackman et al (1995) showed that when abscisic acid was used to activate LEA protein gene expression prematurely in immature soybean seeds, a corresponding improvement in cell integrity was noted after desiccation stress. Over time, many new examples have been defined as LEA proteins on the basis of only one of the above characteristics, i.e.…”

Section: Expression Profilementioning

confidence: 99%

The continuing conundrum of the LEA proteins

Tunnacliffe

Wise

2007

Naturwissenschaften

624

605

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Research into late embryogenesis abundant (LEA) proteins has been ongoing for more than 20 years but, although there is a strong association of LEA proteins with abiotic stress tolerance particularly dehydration and cold stress, for most of that time, their function has been entirely obscure. After their initial discovery in plant seeds, three major groups (numbered 1, 2 and 3) of LEA proteins have been described in a range of different plants and plant tissues. Homologues of groups 1 and 3 proteins have also been found in bacteria and in certain invertebrates. In this review, we present some new data, survey the biochemistry, biophysics and bioinformatics of the LEA proteins and highlight several possible functions. These include roles as antioxidants and as membrane and protein stabilisers during water stress, either by direct interaction or by acting as molecular shields. Along with other hydrophilic proteins and compatible solutes, LEA proteins might also serve as "space fillers" to prevent cellular collapse at low water activities. This multifunctional capacity of the LEA proteins is probably attributable in part to their structural plasticity, as they are largely lacking in secondary structure in the fully hydrated state, but can become more folded during water stress and/or through association with membrane surfaces. The challenge now facing researchers investigating these enigmatic proteins is to make sense of the various in vitro defined functions in the living cell: Are the LEA proteins truly multi-talented, or are they still just misunderstood?

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“…Soluble sugars (Chen and Burris, 1990;Koster and Leopold, 1988) and late embryogenesis-abundant proteins (Blackman et al, 1995;Close, 1996Close, , 1997 are known to accumulate during seed development and are thought to play a role in protecting the embryo during desiccation. It is also well known that endogenous ABA is enhanced during late embryogenesis (Zeevaart and Creelman, 1988;Rock and Quatrano, 1995).…”

Section: Function Of the Peroxisome Channel Proteinmentioning

confidence: 99%