Characterization of a spinach gene responsive to low temperature and water stress

Neven, Lisa; Haskell, Dale; Hofig, Andrea; Li, Qui-Bao; Guy, Charles L.

doi:10.1007/bf00019945

Cited by 132 publications

(99 citation statements)

References 62 publications

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“…Most group 2 LEA/Rab/dehydrin proteins possess only two lysine-rich repeats. The cold-induced spinach CAPS85 protein [23] and the wheat COR39 protein [24] contain 11 and six lysine-rich repeats, respectively. Both proteins lack the serine stretch but COR39 possesses a glycine-rich sequence that is repeated six times.…”

Section: Resultsmentioning

confidence: 99%

Promoter and expression studies on an Arabidopsis thaliana dehydrin gene

1996

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Section: Resultsmentioning

confidence: 99%

Promoter and expression studies on an Arabidopsis thaliana dehydrin gene

1996

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“…DHNs localize primarily to the nucleus or cytoplasm (Houde et al, 1995;Bracale et al, 1997), but studies also corroborate their presence either in the plasma membrane (Danyluk et al, 1998), endoplasmic reticulum (Neven et al, 1993), chloroplast (Wisniewski et al, 1999), mitochondria (Borovskii et al, 2002) or even in the vacuole (Heyen et al, 2002). DHNs may thus be expressed either constitutively [e.g.…”

Section: Structure and Functional Studies Of Dhnamentioning

confidence: 87%

Genetic approaches towards overcoming water deficit in plants - special emphasis on LEAs

Khurana

Vishnudasan

Chhibbar

2008

Physiol Mol Biol Plants

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Water deficit arises as a result of low temperature, salinity and dehydration, thereby affecting plant growth adversely and making it imperative for plants to surmount such situations by acclimatizing/adapting at various levels. Water deficit stress results in significant changes in gene expression, mediated by interconnected signal transduction pathways that may be triggered by calcium, and regulated via ABA dependent and/or independent pathways. Hence, adaptation of plants to such stresses involves maintaining cellular homeostasis, detoxification of harmful elements and also growth alterations. Stress in general cause excess production of reactive oxygen species (ROS) and the plants overcome the same by either preventing the accumulation of ROS or by eliminating the ROS formed. Ion homeostasis includes processes such as cellular uptake, sequestration and export in conjunction with long distance transport. Requisite amounts of osmolytes are hence synthesized under stress to maintain turgor along with maintaining the macromolecular structures and also for scavenging ROS. Another noteworthy response is the accumulation of novel proteins, including enzymes involved in the biosynthesis of osmoprotectants, heat-shock proteins (HSPs), late embryogenesis abundant (LEA) proteins, antifreeze proteins, chaperones, detoxification enzymes, transcription factors, kinases and phosphatases. The LEAs belong to a redundant protein family and are highly hydrophilic, boiling-soluble, non-globular and therefore have been defined and classified accordingly. The precise function of LEAs is still unknown, but substantial evidence indicates their involvement in dessication tolerance as the expression of LEAs confers increased resistance to stress in heterologous yeast system and also significantly improves water deficit tolerance in transgenic plants. Genetic manipulation of plants towards conferring abiotic stress tolerance is a daunting task, as the abiotic stress tolerance mechanism is highly complex and various strategies have been exploited to address and evaluate the stress tolerance mechanism, and the molecular responses to water deficit via complex signaling networks. Genomic technologies have recently been useful in integrating the multigenicity of the plant stress responses through, transcriptomics, proteomics and metabolite profilling and their interactions. This review deals with the recent developments on genetic approaches for water stress tolerance in plants, with special emphasis on LEAs.

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“…In some studies antibodies have been used to examine the expression (Lin and Thomashow, 1992a;Neven et al, 1993;Kazuoka and Oeda, 1994;Boothe et al, 1995;Houde et al, 1995) and to determine the cytological location (Lin and Thomashow, 1992a;Neven et al, 1993;Houde et al, 1995) of low-temperature-induced proteins. In only a few cases have low-temperature-induced proteins been purified (Kazuoka and Oeda, 1994;Houde et al, 1995;Gilmour et al, 1996) and no detailed structural analyses of these proteins have as yet been reported to our knowledge.…”

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confidence: 99%

“…A common feature among many low-temperatureinduced proteins is their tendency to remain soluble following boiling (Lin et al, 1990;Lin and Thomashow, 1992a;Neven et al, 1993). This property is a reflection of the fact that these proteins are extremely hydrophilic, which is also shared by many dehydration-induced proteins.…”

mentioning

confidence: 99%

“…In fact, severa1 of these proteins are induced in response to both low temperature and dehydration. Some low-temperatureinduced proteins also show sequence homology with the group 2 Lea proteins in that they possess repeated stretches of residues rich in Lys (Gilmour et al, 1992;Neven et al, 1993;Kazuoka and Oeda, 1994;Houde et al, 1995). As with other members of the Lea family, the proteins in group 2 are highly hydrophilic and are expressed late in embryogenesis, during the period of seed desiccation (Dure et al, 1989).…”

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confidence: 99%

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Purification, Characterization, and Structural Analysis of a Plant Low-Temperature-Induced Protein

et al. 1997

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We have purified to near homogeneity a recombinant form of the protein BN28 (rBN28), expressed in response to low temperature in Brassica napus plants, and we have determined its solution structure. Antibodies raised against rBN28 were used to characterize the recombinant and native proteins. Similar to many other lowtemperature-induced proteins, BN28 is extremely hydrophilic, such that it remains soluble following boiling. lmmunoblot analysis of subcellular fractions indicated that BN28 was not strongly associated with cellular membranes and was localized exclusively within the soluble fraction of the cell. Contrary to predicted secondary structure that suggested significant helical content, circular dichroism analysis revealed that rBN28 existed in aqueous solution largely as a random coil. However, the helical propensity of the protein could be demonstrated in the presence of trifluoroethanol. Nuclear magnetic resonance analysis further showed that rBN28 was in fact completely unstructured (1 00% coil) in aqueous solution. Although it had earlier been speculated that BN28-like proteins from Arabi-

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Characterization of a spinach gene responsive to low temperature and water stress

Cited by 132 publications

References 62 publications

Promoter and expression studies on an Arabidopsis thaliana dehydrin gene

Promoter and expression studies on an Arabidopsis thaliana dehydrin gene

Genetic approaches towards overcoming water deficit in plants - special emphasis on LEAs

Purification, Characterization, and Structural Analysis of a Plant Low-Temperature-Induced Protein

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