Inactivation of Two Homologues of Proteins Presumed to Be Involved in the Desiccation Tolerance of Plants Sensitizes Deinococcus radiodurans R1 to Desiccation

Battista, John R.; Park, MieJung; McLemore, Andrew E.

doi:10.1006/cryo.2001.2357

Cited by 156 publications

(94 citation statements)

References 17 publications

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“…LEA proteins are not viewed as being restricted to plants anymore, now having been documented in bacteria (26)(27)(28), cyanobacteria (29), slime molds (30), and fungi (31)(32)(33). In addition a steady increase in reports of LEA-like protein in animals has been observed in the last several years.…”

Section: Distribution and Expression Of Lea Proteins In Animalsmentioning

confidence: 99%

LEA Proteins During Water Stress: Not Just for Plants Anymore

Hand

Menze

Toner

et al. 2011

Annu. Rev. Physiol.

363

340

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Section: Distribution and Expression Of Lea Proteins In Animalsmentioning

confidence: 99%

LEA Proteins During Water Stress: Not Just for Plants Anymore

Hand

Menze

Toner

et al. 2011

Annu. Rev. Physiol.

363

340

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“…Multiple LEA proteins are commonly found in a given species, which may be explained in part by targeting to different cellular locations. An organism's expression levels of LEA protein and mRNA are closely tied to its capacity for desiccation tolerance (20)(21)(22)(23)(24)(25)(26). LEA proteins are highly hydrophilic and generally unstructured, with a high percentage of random coils in aqueous solution.…”

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confidence: 99%

Late embryogenesis abundant proteins protect human hepatoma cells during acute desiccation

Chakraborty

Borcar

et al. 2012

Proc. Natl. Acad. Sci. U.S.A.

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Expression of late embryogenesis abundant (LEA) proteins is highly correlated with desiccation tolerance in anhydrobiotic animals, selected land plants, and bacteria. Genes encoding two LEA proteins, one localized to the cytoplasm/nucleus (AfrLEA2) and one targeted to mitochondria (AfrLEA3m), were stably transfected into human HepG2 cells. A trehalose transporter was used for intracellular loading of this disaccharide. Cells were rapidly and uniformly desiccated to low water content (<0.12 g H 2 O/g dry weight) with a recently developed spin-drying technique. Immediately on rehydration, control cells without LEA proteins or trehalose exhibited 0% membrane integrity, compared with 98% in cells loaded with trehalose and expressing AfrLEA2 or AfrLEA3m; surprisingly, AfrLEA3m without trehalose conferred 94% protection. Cell proliferation across 7 d showed an 18-fold increase for cells dried with AfrLEA3m and trehalose, compared with 27-fold for nondried controls. LEA proteins dramatically enhance desiccation tolerance in mammalian cells and offer the opportunity for engineering biostability in the dried state.water stress | biopreservation | intrinsically disordered proteins | osmolyte | Artemia franciscana

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“…A role of LEA proteins in DT has been demonstrated in the bacterium Deinococcus radiodurans. Inactivation of a group 3 LEA protein, homolog of the plant LEA76, leads to 75% reduction in viability of desiccated cultures (Battista et al, 2001). In contrast, in seeds, direct in vivo evidence for a role of LEA proteins in tolerance to complete water loss has not yet been secured.…”

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confidence: 99%

Comparative Analysis of the Heat Stable Proteome of Radicles of Medicago truncatula Seeds during Germination Identifies Late Embryogenesis Abundant Proteins Associated with Desiccation Tolerance

et al. 2006

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A proteomic analysis was performed on the heat stable protein fraction of imbibed radicles of Medicago truncatula seeds to investigate whether proteins can be identified that are specifically linked to desiccation tolerance (DT). Radicles were compared before and after emergence (2.8 mm long) in association with the loss of DT, and after reinduction of DT by an osmotic treatment. To separate proteins induced by the osmotic treatment from those linked with DT, the comparison was extended to 5 mm long emerged radicles for which DT could no longer be reinduced, albeit that drought tolerance was increased. The abundance of 15 polypeptides was linked with DT, out of which 11 were identified as late embryogenesis abundant proteins from different groups: MtEm6 (group 1), one isoform of DHN3 (dehydrins), MtPM25 (group 5), and three members of group 3 (MP2, an isoform of PM18, and all the isoforms of SBP65). In silico analysis revealed that their expression is likely seed specific, except for DHN3. Other isoforms of DNH3 and PM18 as well as three isoforms of the dehydrin Budcar5 were associated with drought tolerance. Changes in the abundance of MtEm6 and MtPM25 in imbibed cotyledons during the loss of DT and in developing embryos during the acquisition of DT confirmed the link of these two proteins with DT. Fourier transform infrared spectroscopy revealed that the recombinant MtPM25 and MtEm6 exhibited a certain degree of order in the hydrated state, but that they became more structured by adopting a helices and b sheets during drying. A model is presented in which DT-linked late embryogenesis abundant proteins might exert different protective functions at high and low hydration levels.

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Inactivation of Two Homologues of Proteins Presumed to Be Involved in the Desiccation Tolerance of Plants Sensitizes Deinococcus radiodurans R1 to Desiccation

Cited by 156 publications

References 17 publications

LEA Proteins During Water Stress: Not Just for Plants Anymore

LEA Proteins During Water Stress: Not Just for Plants Anymore

Late embryogenesis abundant proteins protect human hepatoma cells during acute desiccation

Comparative Analysis of the Heat Stable Proteome of Radicles of Medicago truncatula Seeds during Germination Identifies Late Embryogenesis Abundant Proteins Associated with Desiccation Tolerance

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