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Diverse Accumulation of Several Dehydrin-Like Proteins in Cauliflower (Brassica Oleracea Var

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Diverse Accumulation of Several Dehydrin-Like Proteins in Cauliflower (Brassica Oleracea Var Rurek BMC Plant Biology 2010, 10:181 http://www.biomedcentral.com/1471-2229/10/181 RESEARCH ARTICLE Open Access Diverse accumulation of several dehydrin-like proteins in cauliflower (Brassica oleracea var. botrytis), Arabidopsis thaliana and yellow lupin (Lupinus luteus) mitochondria under cold and heat stress Michal Rurek Abstract Background: Dehydrins represent hydrophilic proteins acting mainly during cell dehydration and stress response. Dehydrins are generally thermostable; however, the so-called dehydrin-like (dehydrin-related) proteins show variable thermolability. Both groups immunoreact with antibodies directed against the K-segment of dehydrins. Plant mitochondrial dehydrin-like proteins are poorly characterized. The purpose of this study was to extend previous reports on plant dehydrins by comparing the level of immunoprecipitated dehydrin-like proteins in cauliflower (Brassica oleracea var. botrytis), Arabidopsis thaliana and yellow lupin (Lupinus luteus) mitochondria under cold and heat stress. Results: All the analyzed plant species showed constitutive accumulation of thermostable mitochondrial putative dehydrins ranging from 50 to 70 kDa. The mitochondrial dehydrin-like proteins observed in cauliflower and Arabidopsis ranged from 10 to 100 kDa and in lupin imbibed seeds and hypocotyls - from 20 to 90 kDa. Cold treatment increased mainly the accumulation of 10-100 kDa cauliflower and Arabidopsis dehydrin-like proteins, in the patterns different in cauliflower leaf and inflorescence mitochondria. However, in lupin mitochondria, cold affected mainly 25-50 kDa proteins and seemed to induce the appearance of some novel dehydrin-like proteins. The influence of frost stress on cauliflower leaf mitochondrial dehydrin- like proteins was less significant. The impact of heat stress was less significant in lupin and Arabidopsis than in cauliflower inflorescence mitochondria. Cauliflower mitochondrial dehydrin-like proteins are localized mostly in the mitochondrial matrix; it seems that some of them may interact with mitochondrial membranes. Conclusions: All the results reveal an unexpectedly broad spectrum of dehydrin-like proteins accumulated during some abiotic stress in the mitochondria of the plant species analyzed. They display only limited similarity in size to those reported previously in maize, wheat and rye mitochondria. Some small thermolabile dehydrin-like proteins were induced under stress conditions applied and therefore they are likely to be involved in stress response. Background in the process of cellular response to stress conditions. Stress acclimation in plants is associated with the LEA proteins show significant evolutionary conservation appearance of characteristic cellular, biochemical and [2,3]. The second group of LEA family, represented by gene expression alterations [1]. It is assumed that the dehydrins, contains hydrophilic, lysine- and glycine-rich LEA protein family is engaged, among other functions, proteins accumulating during seed germination and maturation. Some dehydrins are inducible under differ- Correspondence: [email protected] ent stress conditions such as drought, low temperature, Department of Molecular and Cellular Biology, Institute of Molecular Biology and Biotechnology, Adam Mickiewicz University, Umultowska 89, 61-614 freezing, salinity and ABA treatment [4-7]. Dehydrins Poznan, Poland share the segmental structure, which makes it possible © 2010 Rurek; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. Rurek BMC Plant Biology 2010, 10:181 Page 2 of 17 http://www.biomedcentral.com/1471-2229/10/181 to divide them into five subclasses. All dehydrins con- LEA III family member that is targeted to the pea mito- tain the lysine-rich conserved domain named the K-seg- chondria matrix (shown by functional tests; [21,22]). ment, characterized by the 15- amino acid consensus Interestingly, LEA III family members characterized in motif EKKGIMDKIKEKLPG [4,8]. It is generally wheat and rye chloroplasts displayed elevated accumula- assumed that dehydrins protect the rapidly growing tion under cold stress [23]. plant organs against damage. They are present both in The participation of ‘true’ mitochondrial dehydrin-like the nucleus and in the cytoplasm and also close to the proteins in stress response under cold, drought, frost elements of cytoskeleton as well as in the vicinity of the and ABA treatment was confirmed only recently in cer- plasma membrane and tonoplast [9-13]. The data con- eals. Initially, in winter wheat, winter rye and maize cerning potential associations of dehydrins with other mitochondria, two dlps - of ca. 50 and 60 kDa - were cell compartments are still limited and need more identified [24]. The authors of this paper also showed verification. that during cold stress response, mostly in wheat, the A few members of the dehydrin group were clearly accumulation of the 50 kDa dlp was increased; however, shown to be heat-stable (e.g. the peach PCA60 protein in rye mitochondria this effect concerned 60 kDa pro- [14]) and resistant to structural collapse (e.g. three Ara- tein. It was also proved that the dlps of 50/54 and 60 bidopsis dehydrins [15]). However, numerous related kDa which accumulated in wheat and rye mitochondria proteins - known as ‘dehydrin-like proteins’ (dlps) or were highly thermostable [25]. The same authors also ‘dehydrin-related proteins’ - quite often display variable provided evidence for a positive correlation between the levels of thermostability [16]. The data on their full-size levels of these proteins in rye and wheat mitochondria cDNAs or genomic sequences as well as results of func- in response to cold stress and cold acclimation. They tional analyses are very often unavailable. ‘Dehydrin-like’ suggested that during cold or osmotic stress mitochon- or ‘dehydrin-related proteins’ crossreact with K-segment drial dlps were involved either in the cellular response specific antibodies, which indicates that they may con- against freezing/low temperature or in the regulation of tain a key aminoacid motif- K-segment, similar to the mitochondrial functions [25]. Besides high-molecular one found in dehydrins, with some extent of degenera- weight dlps, the presence of thermolabile lower- mole- tion. In general, ‘dehydrin-like proteins’, immunologi- cular weight dlps in the mitochondrial extracts of winter cally related to dehydrins, are a poorly characterized wheat, rye and maize grown under control conditions group of proteins and they need to be explored thor- was also documented [16]. The authors [16] showed oughly. Nowadays, some of them may be classified as that the wheat and rye proteins of 52 kDa and 63 kDa ‘genuine dehydrins’ rather than as dlps if they share all (recalculation of earlier estimated size of 50 kDa and 60 the properties typical of dehydrins. kDaproteinsbyBorovskiiet al. [24]) were highly accu- Data concerning the occurrence of dehydrins and pro- mulated during the diverse stress conditions; however, teins related to dehydrins in higher plant mitochondria the wheat, rye and maize thermolabile dlps of molecular are very scarce. Recently, using the method of immuno- weight 28 and 56-59 kDa were accumulated in a rather gold tissue staining with antibodies against the K-seg- constitutive manner under the same conditions. The ment of dehydrin, it was shown that constitutive dlps, influence of ABA on thermostable dlps was the highest which associate with the mitochondria of Chenopodium in rye and the lowest in maize mitochondria [16]. The embryonic axes and cotyledons, are active in the seed same authors characterized the interactions of cytoplas- development program [17]. Moreover, the association of mic dehydrins with mitochondria during cold treatment Citrus unshiu cold-responsive COR19 dehydrin - over- of winter wheat plants. According to their results, the expressed in Nicotiana - was observed in the fraction cold-induced winter wheat dehydrin, which displayed an enriched in crude mitochondria [18-20]. The results of elevated level in cytoplasm after acclimation to cold localisation of dehydrin-related proteins contradicted stress, associated rapidly with the mitochondrial outer the other, earlier data obtained from tissue immunogold membrane [26]. staining and Western blot analyses of cellular fractions The aim of the present work was to better understand enriched in mitochondria of other plants [7,9]. Although the function of dlps in plant mitochondria by extending Arabidopsis expression products of ten known dehydrin the above - described studies over three different plant genes ([Gen Bank:NP_173468, NP_850947, NP_175843, species which had not been analyzed previously. Com- NP_177745, NP_179744, NP_190666, NP_190667, parative analysis of the levels of dlps in cauliflower, Ara- NP_195554, NP_195624, NP_201441]) are not predicted bidopsis and yellow lupin mitochondria in response to to be targeted to mitochondria [2], some other plant cold, freeze and heat stress was performed. Also, some LEA proteins could be regarded as putative mitochon- results concerning the association of cauliflower dlps drial proteins [21]. This may be consistent with the with the fraction enriched in membranes are presented recent discovery of a cloned, non-dehydrin, organellar here. Moreover, the influence
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