Binding of a Vitis riparia dehydrin to DNA

Boddington, Kelly F.; Graether, Steffen P.

doi:10.1016/j.plantsci.2019.110172

Cited by 30 publications

(27 citation statements)

References 57 publications

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“…Many LEA proteins have demonstrated the ability to perform multiple functions, termed moonlighting. The COR15 LEA protein can protect both proteins and membranes from freezing damage, 12,65 a citrus LEA protein binds both metal ions and nucleic acids, 28,36 and a V. riparia dehydrin can bind metal ions and protect DNA from oxidative stress 66 . From the in vitro biochemical analyses and disordered nature shown here, it appears that LEA3 proteins may function by providing cryoprotection of enzymes, metal binding and membrane stabilization roles.…”

Section: Discussionmentioning

confidence: 82%

“…The COR15 LEA protein can protect both proteins and membranes from freezing damage, 12,65 a citrus LEA protein binds both metal ions and nucleic acids, 28,36 and a V. riparia dehydrin can bind metal ions and protect DNA from oxidative stress. 66 From the in vitro biochemical analyses and disordered nature shown here, it appears that LEA3 proteins may function by providing cryoprotection of enzymes, metal binding and membrane stabilization roles. Confirmation of these proposals will require further investigation to determine the in vivo role of LEA3 proteins.…”

Section: Discussionmentioning

confidence: 84%

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The in vitro structure and functions of the disordered late embryogenesis abundant three proteins

Singh

Graether

2021

Protein Science

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Late embryogenesis abundant (LEA) proteins are produced during seed embryogenesis and in vegetative tissue in response to various abiotic stressors. A correlation has been established between LEA expression and stress tolerance, yet their precise biochemical mechanism remains elusive. LEA proteins are very rich in hydrophilic amino acids, and they have been found to be intrinsically disordered proteins (IDPs) in vitro. Here, we perform biochemical and structural analyses of the four LEA3 proteins from Arabidopsis thaliana (AtLEA3). We show that the LEA3 proteins are disordered in solution but have regions with propensity for order. All LEA3 proteins were effective cryoprotectants of LDH in the freeze/thaw assays, while only one member, AtLEA3‐4, was shown to bind Cu2+ and Fe3+ ions with micromolar affinity. As well, only AtLEA3‐4 showed binding and a gain in α‐helicity in the presence of the membrane mimic dodecylphosphocholine (DPC). We explored this interaction in greater detail using 15N‐heteronuclear single quantum coherence (HSQC) nuclear magnetic resonance, and demonstrate that two sets of conserved motifs present in AtLEA3‐4 are involved in the interaction with the DPC micelles, which themselves gain α‐helical structure.

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Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 84%

The in vitro structure and functions of the disordered late embryogenesis abundant three proteins

Singh

Graether

2021

Protein Science

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“…•− production in protruding embryonic axes might originate from the abovementioned pathway. Recent studies revealed that dehydrins protect DNA from ROS [69]. Such protection may be sustained in beech elongating embryonic axes at 0-I stages because dehydrins were reported to localize in the nucleus of beech embryonic axes [21].…”

Section: Discussionmentioning

confidence: 99%

Dehydration Sensitivity at the Early Seedling Establishment Stages of the European Beech (Fagus sylvatica L.)

Kalemba

Bagniewska‐Zadworna

Suszka

et al. 2019

Forests

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Shortage of water is a limiting factor for the growth and development of plants, particularly at early developmental stages. We focused on the European beech (Fagus sylvatica L.), which produces seeds and further seedlings in large intervals of up to ten years. To explore the beech seedling establishment process, six stages referring to embryo expansion were studied to determine sensitivity to dehydration. The characterization of the response of elongating embryonic axes and cotyledons included a viability test before and after dehydration and measurement of the amounts of electrolyte leakage, concentration, and arrangement of storage materials, changes in chaperone proteins related to water deficit, and accumulation of hydrogen peroxide and superoxide anion radicals. Elongating embryonic axes and cotyledons differed in water content, dehydration rates, membrane permeability before and after dehydration, protein, and lipid decomposition pattern, and amount of 44-kDa dehydrin and 22-kDa small heat shock protein (sHSP). Protruding embryonic axes were more sensitive to dehydration than cotyledons, although dehydration caused transient reinduction of three dehydrin-like proteins and sHSP synthesis, which accompany desiccation tolerance. Extended deterioration, including overproduction of hydrogen peroxide and depletion of superoxide anion radicals, was reported in dehydrated embryonic axes longer than 10 mm characterized by highly elevated cellular leakage. The apical part elongating embryonic axes consisting of the radicles was the most sensitive part of the seed to dehydration, and the root apical meristem area was the first to become inviable. The effects of severe dehydration involving ROS imbalance and reduced viability in beech seedlings with embryonic axes longer than 10 mm might help to explain the difficulties in beech seedling establishment observed in drought-affected environments. The conversion of environmental drought into climate-originated oxidative stress affecting beech seedling performance is discussed in this report.

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“…Evidently, many different functions have been suggested for LEA proteins and it is becoming more apparent that some LEA proteins can perform multiple functions. A mitochondria pea LEA protein and the chloroplast LEA protein COR15 can protect both proteins and membranes (Lin and Thomashow, 1992;Nakayama et al, 2007), a citrus LEA protein can bind metal ions and nucleic acids (Hara et al, 2005;Hara et al, 2009), and a grapevine LEA protein can bind metals and also DNA to protect it from oxidative stress (Boddington and Graether, 2019). The ability of LEA proteins to perform multiple functions is termed "moonlighting" and is a common characteristic of IDPs; their structural heterogeneity may be associated with greater functional promiscuity (Tompa, 2005).…”

Section: Other Functionsmentioning

confidence: 99%

Expression and Purification of an Intrinsically Disordered Protein

Singh

Graether

2020

Methods in Molecular Biology

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LEA3 proteins are intrinsically disordered proteins expressed during seed development and in response to abiotic stress. Limited studies have shown they can confer stress tolerance in plants, yet their mechanism remains elusive. This thesis aims to further our understanding of the LEA3 group. First, a comprehensive bioinformatics analysis revealed two previously undiscovered C-terminal motifs containing conserved acidic and hydrophobic residues and four N-terminal motifs. Five general architectures were proposed for LEA3 and the physiochemical properties of the different architectures showed clustering in a relatively narrow range compared to the previously studied dehydrins. The evolutionary analysis revealed that the proteins grouped into clades based on their architecture, and that there appears to be at least two distinct groups of LEA3 proteins based on their architectures and physiochemical properties. The presence of LEA3 proteins in non-vascular plants but their absence in algae suggests that LEA3 may have arose in the evolution of land plants. A protocol to express and purify AtLEA3-2 with 15 N and 13 C isotopes in E. coli is described, although the protocol can be adapted for any LEA3 with or without isotopic labeling. The AtLEA 3-2 gene was cloned into the pET-SUMO vector, which allowed for the SUMO-AtLEA 3-2 fusion protein to be purified using Ni-affinity chromatography and, through the use of Ulp1, a

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Binding of a Vitis riparia dehydrin to DNA

Cited by 30 publications

References 57 publications

The in vitro structure and functions of the disordered late embryogenesis abundant three proteins

The in vitro structure and functions of the disordered late embryogenesis abundant three proteins

Dehydration Sensitivity at the Early Seedling Establishment Stages of the European Beech (Fagus sylvatica L.)

Expression and Purification of an Intrinsically Disordered Protein

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