A diurnally regulated dehydrin from Avicennia marina that shows nucleo-cytoplasmic localization and is phosphorylated by Casein kinase II in vitro

Mehta, Preeti; Rebala, Keerthi C.; Venkataraman, Gayatri; Parida, Ajay

doi:10.1016/j.plaphy.2009.03.008

Cited by 31 publications

(16 citation statements)

References 41 publications

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“…In addition to low molecular osmolytes, an increased biosynthesis of several hydrophilic proteins with osmoprotective function (e.g., proteins from LEA superfamily including dehydrins) has been found (reviewed in [44,107,108]). As examples of salt-inducible LEA proteins, dehydrin TAS14 in tomato [93], several dehydrins and LEA3 proteins in salt-tolerant Indica rice cultivars Pokkali and Nona Bokra [94], phosphorylated DHN5 in durum wheat [95], PeuDHN1 in poplar Populus euramericana [92] and AmDHN1 in gray mangrove Avicennia marina [33] can be given. Plants thus solve the problem of a decrease in ambient osmotic potential by accumulation of newly synthesized organic compounds; in contrast, a tight regulation of inorganic salt ions occurs in salt-treated plants.…”

Section: Proteomic Level Of Adaptation To Salinitymentioning

confidence: 99%

“…Two lengths of arrows were used in the scheme; in case of short arrows, the quantitative change in protein abundance in proteins involved in a given process is generally smaller than in case of long arrows. References: ( A ) Signalling [19,21,22,89]; ( B ) Salinity-responsive gene expression [22,76,91]; ( C ) Protein biosynthesis [22,59,61]; ( D ) Energy metabolism [22,23,61]; ( E ) Oxidative stress [60,72,74]; ( F ) Protein degradation [26,60,70,78]; ( G ) Anaerobic metabolism [56,58,73]; ( H , I ) Saccharide catabolism; TCA cycle, respiration [22,28,62]; ( J ) Photosynthesis [16,26,29]; ( K ) ATP biosynthesis [22,61,70,86,88]; ( L ) Ion transport [22–24,51,57,82,87]; ( M ) Antioxidants [22,23,28,60,61,72,76,80,88,89]; ( N ) Chaperones [22,25,72,74,75,81,84,89,92]; ( O ) LEA proteins [33,92–95]; ( P ) Osmolyte biosynthesis [19,…”

Section: Figurementioning

confidence: 99%

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Protein Contribution to Plant Salinity Response and Tolerance Acquisition

Kosová

Prášil

Vítámvás

2013

IJMS

179

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The review is focused on plant proteome response to salinity with respect to physiological aspects of plant salt stress response. The attention is paid to both osmotic and ionic effects of salinity stress on plants with respect to several protein functional groups. Therefore, the role of individual proteins involved in signalling, changes in gene expression, protein biosynthesis and degradation and the resulting changes in protein relative abundance in proteins involved in energy metabolism, redox metabolism, stressand defence-related proteins, osmolyte metabolism, phytohormone, lipid and secondary metabolism, mechanical stress-related proteins as well as protein posttranslational modifications are discussed. Differences between salt-sensitive (glycophytes) and salt-tolerant (halophytes) plants are analysed with respect to differential salinity tolerance. In conclusion, contribution of proteomic studies to understanding plant salinity tolerance is summarised and discussed.

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Section: Proteomic Level Of Adaptation To Salinitymentioning

confidence: 99%

Section: Figurementioning

confidence: 99%

Protein Contribution to Plant Salinity Response and Tolerance Acquisition

Kosová

Prášil

Vítámvás

2013

IJMS

179

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“…The S-segment is a variable length motif consisting of a tract of Ser residues (Close, 1996). It is a phosphorylation site and has been theorized to require a C-terminal acidic region in order to be phosphorylated (Mehta et al, 2009). The phosphorylated S-segment has been shown to cause dehydrin translocation from the cytoplasm to the nucleus (Goday et al, 1994), and also to increase the calcium binding capacity of the protein (Alsheikh et al, 2003).…”

Section: Introductionmentioning

confidence: 99%

Genome Analysis of Conserved Dehydrin Motifs in Vascular Plants

et al. 2017

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Dehydrins, a large family of abiotic stress proteins, are defined by the presence of a mostly conserved motif known as the K-segment, and may also contain two other conserved motifs known as the Y-segment and S-segment. Using the dehydrin literature, we developed a sequence motif definition of the K-segment, which we used to create a large dataset of dehydrin sequences by searching the Pfam00257 dehydrin dataset and the Phytozome 10 sequences of vascular plants. A comprehensive analysis of these sequences reveals that lysine residues are highly conserved in the K-segment, while the amino acid type is often conserved at other positions. Despite the Y-segment name, the central tyrosine is somewhat conserved, but can be substituted with two other small aromatic amino acids (phenylalanine or histidine). The S-segment contains a series of serine residues, but in some proteins is also preceded by a conserved LHR sequence. In many dehydrins containing all three of these motifs the S-segment is linked to the K-segment by a GXGGRRKK motif (where X can be any amino acid), suggesting a functional linkage between these two motifs. An analysis of the sequences shows that the dehydrin architecture and several biochemical properties (isoelectric point, molecular mass, and hydrophobicity score) are dependent on each other, and that some dehydrin architectures are overexpressed during certain abiotic stress, suggesting that they may be optimized for a specific abiotic stress while others are involved in all forms of dehydration stress (drought, cold, and salinity).

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“…Some dehydrins can also be expressed constitutively during normal growth (Rodriguez et al 2005;Rorat et al 2004Rorat et al , 2006. Under stress conditions, DHNs accumulate in most tissues and cells and are mainly localized to the cytoplasm and nucleus of the plant cell (Close 1997;Mehta et al 2009;Rorat 2006;Tunnacliffe and Wise 2007), although some DHNs have been found to interact with the chloroplasts (Mueller et al 2003), mitochondria (Borovskii et al 2002), plasma membrane (Danyluk et al 1998;Puhakainen et al 2004), and tonoplasts (Heyen et al 2002;Saavedra et al 2006). Such a wide distribution and expression pattern suggests that these proteins play essential roles in plant growth and stress tolerance.…”

Section: Introductionmentioning

confidence: 99%

Overexpression of a maize dehydrin gene, ZmDHN2b, in tobacco enhances tolerance to low temperature

et al. 2011

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Dehydrins, a subfamily of group 2 LEA proteins, are intrinsically unstructured plant proteins that accumulate in the late stages of seed development and in vegetative tissues subjected to water deficit, salinity, low temperature, or abscisic acid treatment. In this study, we isolated and characterized ZmDHN2b, a maize dehydrin gene. The genomic organization of the ZmDHN2b gene and its expression in maize seedlings were analyzed. To investigate the function of ZmDHN2b, we generated transgenic tobacco plants constitutively overexpressing ZmDHN2b. Ectopic expression of ZmDHN2b in tobacco accelerated seed germination and seedling growth at 15°C. Furthermore, ZmDHN2b-overexpressing lines had lower levels of coldinduced malondialdehyde and less electrolyte leakage than wild-type tobacco at 4°C. These results demonstrated that ZmDHN2b was involved in plant responses to low temperature.

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A diurnally regulated dehydrin from Avicennia marina that shows nucleo-cytoplasmic localization and is phosphorylated by Casein kinase II in vitro

Cited by 31 publications

References 41 publications

Protein Contribution to Plant Salinity Response and Tolerance Acquisition

Protein Contribution to Plant Salinity Response and Tolerance Acquisition

Genome Analysis of Conserved Dehydrin Motifs in Vascular Plants

Overexpression of a maize dehydrin gene, ZmDHN2b, in tobacco enhances tolerance to low temperature

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