Plant Hsp100 family with special reference to rice

Heat shock proteins (Hsps) represent a group of specific proteins which are synthesized primarily in response to heat shock in almost all biological systems. Members of Hsp100 family have been directly implicated in induction of thermotolerance in microbial and animal cells. Yeast cells harbouring defective hsp104 gene do not show thermotolerance under conditions in which the normal cells do. Several plant species have been shown to synthesize Hsps in the range of 100 kDa. Rice Hsp104 (OsHsp104) is rapidly and predominantly accumulated in heat-shocked cells. Western blotting analysis show that anti rice Hsp104 antibodies (generated against purified Hsp104 protein from cultivated rice Oryza sativa L.) cross-react with the same-sized high temperature inducible protein in 15 different wild rices. It was further found that anti rice Hsp104 antibodies also cross-react with a major high temperature regulated protein ofEscherichia coli. We have previously shown that a 110 kDa stress regulated protein in rice (OsHsp110) is immunologically related to yeast Hsp104 protein. In this paper, we present a comparative account of characteristics of the OsHsp104 and OsHsp110 proteins

Oxidative environment and redox homeostasis in plants: dissecting out significant contribution of major cellular organelles

Plant cells are often exposed to oxidative cellular environments which result in the generation of toxic reactive oxygen species (ROS). In order to detoxify the harmful ROS, plants have evolved various strategies including their scavenging and antioxidant machinery. Plant cells contain many enzymatic and non-enzymatic antioxidants which aid in removing the toxic oxygen molecules. Various antioxidant molecules localized within different cellular compartments play crucial role(s) during this process, which includes both redox-signalling and redox-homeostasis. The present review gives an overview of cellular oxidative environment, redox signalling operative within a cell and contributions of major cellular organelles towards maintaining the redox homeostasis. Additionally, the importance of various antioxidant enzymes working in an orchestrated and coordinated manner within a cell, to protect it from stress injury has been presented. We also present the state-of-the-art where transgenic approach has been used to improve stress tolerance in model and crop species by engineering one or more than one of these components of the ROS scavenging machinery

OsSRO1a Interacts with RNA Binding Domain-Containing Protein (OsRBD1) and Functions in Abiotic Stress Tolerance in Yeast

SRO1 is an important regulator of stress and hormonal response in plants and functions by interacting with transcription factors and several other proteins involved in abiotic stress response. In the present study, we report OsRBD1, an RNA Binding Domain 1- containing protein as a novel interacting partner of OsSRO1a from rice. The interaction of OsSRO1a with OsRBD1 was shown in yeast as well as in planta. Domain-Domain interaction study revealed that C-terminal RST domain of OsSRO1a interacts with the N-terminal RRM1 domain of OsRBD1 protein. Both the proteins were found to co-localize in nucleus. Transcript profiling under different stress conditions revealed co-regulation of OsSRO1a and OsRBD1 expression under some abiotic stress conditions. Further, co-transformation of both OsSRO1a and OsRBD1 in yeast conferred enhanced tolerance towards salinity, osmotic and methylglyoxal treatments. Our study suggests that the interaction of OsSRO1a with OsRBD1 confers enhanced stress tolerance in yeast and may play an important role under abiotic stress responses in plants

Episodes of horizontal gene-transfer and gene-fusion led to co-existence of different metal-ion specific glyoxalase I

Glyoxalase pathway plays an important role in stress adaptation and many clinical disorders. The first enzyme of this pathway, glyoxalase I (GlxI), uses methylglyoxal as a substrate and requires either Ni(II)/Co(II) or Zn(II) for activity. Here we have investigated the origin of different metal ion specificities of GlxI and subsequent pattern of inheritance during evolution. Our results suggest a primitive origin of single-domain Ni dependent GlxI [Ni-GlxI]. This subsequently evolved into Zn activated GlxI [Zn-GlxI] in deltaproteobacteria. However, origin of eukaryotic Zn-GlxI is different and can be traced to GlxI from Candidatus pelagibacter and Sphingomonas. In eukaryotes GlxI has evolved as two-domain protein but the corresponding Zn form is lost in plants/higher eukaryotes. In plants gene expansion has given rise to multiple two-domain Ni-GlxI which are differentially regulated under abiotic stress conditions. Our results suggest that different forms of GlxI have evolved to help plants adapt to stress

Transcriptional Downregulation of Rice rpL32 Gene under Abiotic Stress Is Associated with Removal of Transcription Factors within the Promoter Region

Background: The regulation of ribosomal proteins in plants under stress conditions has not been well studied. Although a few reports have shown stress-specific post-transcriptional and translational mechanisms involved in downregulation of ribosomal proteins yet stress-responsive transcriptional regulation of ribosomal proteins is largely unknown in plants. Methodology/Principal Findings: In the present work, transcriptional regulation of genes encoding rice 60S ribosomal protein L32 (rpL32) in response to salt stress has been studied. Northern and RT-PCR analyses showed a significant downregulation of rpL32 transcripts under abiotic stress conditions in rice. Of the four rpL32 genes in rice genome, the gene on chromosome 8 (rpL32_8.1) showed a higher degree of stress-responsive downregulation in salt sensitive rice variety than in tolerant one and its expression reverted to its original level upon withdrawal of stress. The nuclear run-on and promoter:reporter assays revealed that the downregulation of this gene is transcriptional and originates within the promoter region. Using in vivo footprinting and electrophoretic mobility shift assay (EMSA), cis-elements in the promoter of rpL32_8.1 showing reduced binding to proteins in shoots of salt stressed rice seedlings were identified. Conclusions: The present work is one of the few reports on study of stress downregulated genes. The data revealed that rpL32 gene is transcriptionally downregulated under abiotic stress in rice and that this transcriptional downregulation i

Short-term salinity and high temperature stress-associated ultrastructural alterations in young leaf cells of Oryza sativa L

Salinity and high temperature stresses adversely affect growth and development of rice plants. To investigate the response of rice cells to these stresses, we have analysed short-term stress-induced subcellular alterations in undifferentiated leaf cells of rice seedlings by transmission electron microscopy. Perturbations noted particularly with respect to plasma membrane, mitochondrial membranes, endoplasmic reticulum, polyribosomes and dictyosomes are highlighted. The subcellular changes evoked by both stresses after 4 h were lysis of the cytoplasm, accumulation of electron-dense granules in the cytoplasm, distension in the ER membranes, enhanced association of ribosomes with the endoplasmic reticulum, reduction in the number of mitochondrial cristae, as well as disorganization of cell wall fibrillar material. Certain changes were found to be unique to either the salinity or high temperature stress. Plasmolysis and increased cytoplasmic vesiculation were seen only in response to salinity stress, while discontinuity in the plasma membrane with close association of the osmiophilic granules were observed only in response to high temperature

Plant Hsp90 family with special reference to rice

Hsp90 family represents a group of highly conserved and strongly expressed proteins present in almost all biological species. Heat shock proteins in the range of 90 kDa have been detected in a range of plant species andhsp90 genes have been cloned and characterized in selected instances. However, the expression characteristics of plant Hsp90 are poorly understood. Work on expression characteristics of rice Hsp90 is reviewed in this paper. Experimental evidence is provided for indicating that while the rice 87 kDa protein is transiently synthesized within initial 2 h of heat shock, high steady-state levels of this protein are retained even under prolonged high temperature stress conditions or recovery following 4 h heat shock. It is further shown that fifteen different wild rices accumulate differential levels of these proteins in response to heat shock treatment

Yeast HSP104 homologue rice HSP110 is developmentally- and stress-regulated

HSP104 plays a critical role in the development of thermotolerance in yeast cells. Rice (Oryza sativa L.) HSP110 (OsHSP110) is previously shown to be an immunological homologue of yeast HSP104. This protein accumulates in rice seedlings in response to heat shock. However, no such high temperature-induced accumulation of OsHSP110 was found in the topmost leaf of 90-day-old (just prior to flowering) plants of the cultivated species of rice (Oryza sativa L.) in our earlier study. In this paper, we show that, at the comparable growth stage, leaves of O. australiensis accumulated this protein to a marginal extent in response to heat shock, while levels of HSP110 were either markedly declined or remained unaltered in 14 other wild rice species. Further, different organs of the mature cultivated rice plant accumulated differential levels of OsHSP110, constitutively as well as in response to heat shock. In particular, upper portions of culm, grains and developing embryos showed significantly high constitutive levels of OsHSP110. Tissue print immunolocalization studies showed that OsHSP110 is distributed in the vascular bundles in the shoot tissues and in seeds it is specifically localized in the seec coat (outermost layer) only. Importantly, OsHSP110 accumulated in shoots of rice seedlings in response to salinity, desiccation and low temperature stress also; furthermore, salinity stress (NaCl) caused nearly a three-fold higher accumulation of this protein than high temperature stress

Immunological evidence for accumulation of two high-molecular-weight (104 and 90 kDa) HSPs in response to different stresses in rice and in response to high temperature stress in diverse plant genera

Rice seedlings accumulate stainable amounts of the 104 and 90 kDa polypeptides in response to high temperature stress. We have purified and raised highly specific polyclonal antisera against both of these polypeptides. In western blotting experiments, we find that these proteins are accumulated to different extents in rice seedlings subjected to salinity (NaCl), water stress, low-temperature stress and exogenous abscisic acid application. These proteins also accumulated when rice seedlings grown in pots under natural conditions were subjected to water stress by withholding watering. Seedlings of Triticum aestivum, Sorghum bicolor, Pisum sativum, Zea mays, Brassica juncea and mycelium of Neurospora crassa showed accumulation of the immunological homologues of both the 104 and the 90 kDa polypeptides, in response to high-temperature stress. We have earlier shown that shoots of rice seedlings exposed to heat shock accumulate a 110 kDa polypeptide which is an immunological homologue of the yeast HSP 104 (Singla and Grover, Plant Mol Biol 22: 1177-1180, 1993). Employing anti-rice HSP 104 antibodies and anti-yeast HSP 104 antibodies together, we provide evidence that rice HSP 104 is different from the earlier characterized rice HSP 110