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Journal ArticleDOI

Regulation of the Heat-Shock Response

01 Aug 1998-Plant Physiology (American Society of Plant Biologists)-Vol. 117, Iss: 4, pp 1135-1141
TL;DR: The heat-shock response is a conserved reaction of cells and organisms to elevated temperatures (heat shock or heat stress).
Abstract: The heat-shock response is a conserved reaction of cells and organisms to elevated temperatures (heat shock or heat stress). Whereas severe heat stress leads to cellular damage and cell death, sublethal doses of heat stress induce a cellular response, the heat-shock response, which (a) protects
Citations
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Journal ArticleDOI
26 Sep 2003-Planta
TL;DR: The present review summarizes the recent advances in elucidating stress-response mechanisms and their biotechnological applications and examines the following aspects: regulatory controls, metabolite engineering, ion transport, antioxidants and detoxification, late embryogenesis abundant (LEA) and heat-shock proteins.
Abstract: Abiotic stresses, such as drought, salinity, extreme temperatures, chemical toxicity and oxidative stress are serious threats to agriculture and the natural status of the environment. Increased salinization of arable land is expected to have devastating global effects, resulting in 30% land loss within the next 25 years, and up to 50% by the year 2050. Therefore, breeding for drought and salinity stress tolerance in crop plants (for food supply) and in forest trees (a central component of the global ecosystem) should be given high research priority in plant biotechnology programs. Molecular control mechanisms for abiotic stress tolerance are based on the activation and regulation of specific stress-related genes. These genes are involved in the whole sequence of stress responses, such as signaling, transcriptional control, protection of membranes and proteins, and free-radical and toxic-compound scavenging. Recently, research into the molecular mechanisms of stress responses has started to bear fruit and, in parallel, genetic modification of stress tolerance has also shown promising results that may ultimately apply to agriculturally and ecologically important plants. The present review summarizes the recent advances in elucidating stress-response mechanisms and their biotechnological applications. Emphasis is placed on transgenic plants that have been engineered based on different stress-response mechanisms. The review examines the following aspects: regulatory controls, metabolite engineering, ion transport, antioxidants and detoxification, late embryogenesis abundant (LEA) and heat-shock proteins.

3,248 citations

Journal ArticleDOI
15 Dec 2000-Science
TL;DR: The completion of the Arabidopsis thaliana genome sequence allows a comparative analysis of transcriptional regulators across the three eukaryotic kingdoms and reveals the evolutionary generation of diversity in the regulation of transcription.
Abstract: The completion of the Arabidopsis thaliana genome sequence allows a comparative analysis of transcriptional regulators across the three eukaryotic kingdoms. Arabidopsis dedicates over 5% of its genome to code for more than 1500 transcription factors, about 45% of which are from families specific to plants. Arabidopsis transcription factors that belong to families common to all eukaryotes do not share significant similarity with those of the other kingdoms beyond the conserved DNA binding domains, many of which have been arranged in combinations specific to each lineage. The genome-wide comparison reveals the evolutionary generation of diversity in the regulation of transcription.

2,582 citations

Journal ArticleDOI
TL;DR: The primary effect of low RWC on Apot is most probably caused by limited RuBP synthesis, as a result of decreased ATP synthesis, either through inhibition of Coupling Factor activity or amount due to increased ion concentration.
Abstract: Summary Experimental studies on CO2 assimilation of mesophytic C3 plants in relation to relative water content (RWC) are discussed. Decreasing RWC slows the actual rate of photosynthetic CO2 assimilation (A) and decreases the potential rate (Apot). Generally, as RWC falls from c. 100 to c. 75%, the stomatal conductance (gs) decreases, and with it A. However, there are two general types of relation of Apot to RWC, which are called Type 1 and Type 2. Type 1 has two main phases. As RWC decreases from 100 to c. 75%, Apot is unaffected, but decreasing stomatal conductance (gs) results in smaller A, and lower CO2 concentration inside the leaf (Ci) and in the chloroplast (Cc), the latter falling possibly to the compensation point. Down-regulation of electron transport occurs by energy quenching mechanisms, and changes in carbohydrate and nitrogen metabolism are considered acclimatory, caused by low Ci and reversible by elevated CO2. Below 75% RWC, there is metabolic inhibition of Apot, inhibition of A then being partly (but progressively less) reversible by elevated CO2; gs regulates A progressively less, and Ci and CO2 compensation point, Γ rise. It is suggested that this is the true stress phase, where the decrease in Apot is caused by decreased ATP synthesis and a consequent decreased synthesis of RuBP. In the Type 2 response, Apot decreases progressively at RWC 100 to 75%, with A being progressively less restored to the unstressed value by elevated CO2. Decreased gs leads to a lower Ci and Cc but they probably do not reach compensation point: gs becomes progressively less important and metabolic limitations more important as RWC falls. The primary effect of low RWC on Apot is most probably caused by limited RuBP synthesis, as a result of decreased ATP synthesis, either through inhibition of Coupling Factor activity or amount due to increased ion concentration. Carbohydrate synthesis and accumulation decrease. Type 2 response is considered equivalent to Type 1 at RWC below c. 75%, with Apot inhibited by limited ATP and RuBP synthesis, respiratory metabolism dominates and Ci and Γ rise. The importance of inhibited ATP synthesis as a primary cause of decreasing Apot is discussed. Factors determining the Type 1 and Type 2 responses are unknown. Electron transport is maintained (but down-regulated) in Types 1 and 2 over a wide range of RWC, and a large reduced/oxidized adenylate ratio results. Metabolic imbalance results in amino acid accumulation and decreased and altered protein synthesis. These conditions profoundly affect cell functions and ultimately cause cell death. Type 1 and 2 responses may reflect differences in gs and in sensitivity of metabolism to decreasing RWC.

1,791 citations

Journal ArticleDOI
TL;DR: The authors showed that H2O2 is a potent activator of mitogen-activated protein kinases (MAPKs) in Arabidopsis leaf cells using epitope tagging and a protoplast transient expression assay.
Abstract: Despite the recognition of H2O2 as a central signaling molecule in stress and wounding responses, pathogen defense, and regulation of cell cycle and cell death, little is known about how the H2O2 signal is perceived and transduced in plant cells We report here that H2O2 is a potent activator of mitogen-activated protein kinases (MAPKs) in Arabidopsis leaf cells Using epitope tagging and a protoplast transient expression assay, we show that H2O2 can activate a specific Arabidopsis mitogen-activated protein kinase kinase kinase, ANP1, which initiates a phosphorylation cascade involving two stress MAPKs, AtMPK3 and AtMPK6 Constitutively active ANP1 mimics the H2O2 effect and initiates the MAPK cascade that induces specific stress-responsive genes, but it blocks the action of auxin, a plant mitogen and growth hormone The latter observation provides a molecular link between oxidative stress and auxin signal transduction Finally, we show that transgenic tobacco plants that express a constitutively active tobacco ANP1 orthologue, NPK1, display enhanced tolerance to multiple environmental stress conditions without activating previously described drought, cold, and abscisic acid signaling pathways Thus, manipulation of key regulators of an oxidative stress signaling pathway, such as ANP1/NPK1, provides a strategy for engineering multiple stress tolerance that may greatly benefit agriculture

1,478 citations

Journal ArticleDOI
28 Oct 1999-Nature
TL;DR: It is shown that ATP-synthase (coupling factor) decreases with stress and concluded that photosynthetic assimilation of CO2 by stressed leaves is not limited by CO2 diffusion but by inhibition of ribulose biphosphate synthesis, related to lower ATP content resulting from loss of ATP synthase.
Abstract: Water stress substantially alters plant metabolism, decreasing plant growth and photosynthesis1,2,3,4 and profoundly affecting ecosystems and agriculture, and thus human societies5 There is controversy over the mechanisms by which stress decreases photosynthetic assimilation of CO2 Two principal effects are invoked2,4: restricted diffusion of CO2 into the leaf, caused by stomatal closure6,7,8, and inhibition of CO2 metabolism9,10,11 Here we show, in leaves of sunflower (Helianthus annuus L), that stress decreases CO2 assimilation more than it slows O2 evolution, and that the effects are not reversed by high concentrations of CO212,13 Stress decreases the amounts of ATP9,11 and ribulose bisphosphate found in the leaves, correlating with reduced CO2 assimilation11, but the amount and activity of ribulose bisphosphate carboxylase-oxygenase (Rubisco) do not correlate We show that ATP-synthase (coupling factor) decreases with stress and conclude that photosynthetic assimilation of CO2 by stressed leaves is not limited by CO2 diffusion but by inhibition of ribulose biphosphate synthesis, related to lower ATP content resulting from loss of ATP synthase

885 citations

References
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Journal ArticleDOI
TL;DR: Analysis of HSF cDNA clones from many species has defined structural and regulatory regions responsible for the inducible activities of the conserved heat shock transcription factor.
Abstract: Organisms respond to elevated temperatures and to chemical and physiological stresses by an increase in the synthesis of heat shock proteins. The regulation of heat shock gene expression in eukaryotes is mediated by the conserved heat shock transcription factor (HSF). HSF is present in a latent state under normal conditions; it is activated upon heat stress by induction of trimerization and high-affinity binding to DNA and by exposure of domains for transcriptional activity. Analysis of HSF cDNA clones from many species has defined structural and regulatory regions responsible for the inducible activities. The heat stress signal is thought to be transduced to HSF by changes in the physical environment, in the activity of HSF-modifying enzymes, or by changes in the intracellular level of heat shock proteins.

1,215 citations

01 Jan 1990
TL;DR: Only for you today!
Abstract: Only for you today! Discover your favourite stress proteins in biology and medicine book right here by downloading and getting the soft file of the book. This is not your time to traditionally go to the book stores to buy a book. Here, varieties of book collections are available to download. One of them is this stress proteins in biology and medicine as your preferred book. Getting this book b on-line in this site can be realized now by visiting the link page to download. It will be easy. Why should be here?

811 citations

Journal ArticleDOI
10 Feb 1994-Nature
TL;DR: The chromatin structure of the hsp70 promoter is reconstructed using an in vitro nucleosome assembly system, suggesting that an energy-dependent pathway is involved in chromatin remodelling.
Abstract: Genetic control elements are usually situated in local regions of chromatin that are hypersensitive to structural probes such as DNase I. We have reconstructed the chromatin structure of the hsp70 promoter using an in vitro nucleosome assembly system. Binding of the GAGA transcription factor on existing nucleosomes leads to nucleosome disruption, DNase I hypersensitivity at the TATA box and heat-shock elements, and rearrangement of adjacent nucleosomes. ATP hydrolysis facilitates this process, suggesting that an energy-dependent pathway is involved in chromatin remodelling.

661 citations

Journal ArticleDOI
TL;DR: This review summarizes the current understanding of how molecular chaperones function in plants, with a major focus on those systems where the most detailed mechanistic data are available, or where features of the chaperone/foldase system or substrate proteins are unique to plants.
Abstract: Protein folding in vivo is mediated by an array of proteins that act either as ‘foldases’ or ‘molecular chaperones’. Foldases include protein disulfide isomerase and peptidyl prolyl isomerase, which catalyze the rearrangement of disulfide bonds or isomerization of peptide bonds around Pro residues, respectively. Molecular chaperones are a diverse group of proteins, but they share the property that they bind substrate proteins that are in unstable, non-native structural states. The best understood chaperone systems are HSP70/DnaK and HSP60/GroE, but considerable data support a chaperone role for other proteins, including HSP100, HSP90, small HSPs and calnexin. Recent research indicates that many, if not all, cellular proteins interact with chaperones and/or foldases during their lifetime in the cell. Different chaperone and foldase systems are required for synthesis, targeting, maturation and degradation of proteins in all cellular compartments. Thus, these diverse proteins affect an exceptionally broad array of cellular processes required for both normal cell function and survival of stress conditions. This review summarizes our current understanding of how these proteins function in plants, with a major focus on those systems where the most detailed mechanistic data are available, or where features of the chaperone/foldase system or substrate proteins are unique to plants.

596 citations

Journal ArticleDOI
08 Jan 1993-Science
TL;DR: The results suggest that the carboxyl-terminal zipper may suppress formation of trimers by the amino- terminal HSF zipper elements by means of intramolecular coiled-coil interactions that are sensitive to heat shock.
Abstract: The human and Drosophila heat shock transcription factors (HSFs) are multi-zipper proteins with high-affinity binding to DNA that is regulated by heat shock-induced trimerization. Formation of HSF trimers is dependent on hydrophobic heptad repeats located in the amino-terminal region of the protein. Two subregions at the carboxyl-terminal end of human HSF1 were identified that maintain the monomeric form of the protein under normal conditions. One of these contains a leucine zipper motif that is conserved between vertebrate and insect HSFs. These results suggest that the carboxyl-terminal zipper may suppress formation of trimers by the amino-terminal HSF zipper elements by means of intramolecular coiled-coil interactions that are sensitive to heat shock.

498 citations