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Cca-miR398 increases copper sulfate stress sensitivity via the regulation of CSD mRNA transcription levels in transgenic Arabidopsis thaliana

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MicroRNAs play crucial roles during the process of plant development under stress conditions. Copper is an essential micronutrient for most organisms and serves as an important redox-active cofactor for various functional proteins. In the present study, we investigated the effects of copper sulfate

Single-stranded nucleic acid binding in Arabidopsis thaliana cold shock protein is cold shock domain dependent.

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Cold shock proteins (CSPs) are ancient nucleic acid-binding proteins and well conserved from bacteria to animals as well as plants. In prokaryotes, CSPs possess a single cold shock domain (CSD) while animal CSPs, flanked by N- and C-terminal domains, are commonly named Y-box proteins. Interestingly,

The C-terminal zinc finger domain of Arabidopsis cold shock domain proteins is important for RNA chaperone activity during cold adaptation.

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Among the four cold shock domain proteins (CSDPs) identified in Arabidopsis thaliana, it has recently been shown that CSDP1 harboring seven CCHC-type zinc fingers, but not CSDP2 harboring two CCHC-type zinc fingers, function as a RNA chaperone during cold adaptation. However, the structural features

[Cold shock domain proteins in the extremophyte Thellungiella salsuginea (salt cress): gene structure and differential response to cold].

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Four genes encoding cold shock domain (CSD) proteins have been identified in salt cress [Thellungiella salsuginea (halophila), an extremophyte currently recognized as a promising model for studying stress tolerance]. The deduced proteins prove highly homologous to those of Arabidopsis thaliana (up

[Identification and nucleotide polymorphisms in Brassica rapa genes coding cold shock domain proteins (CSDP)].

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Full-length BrCSDP2 and BrCSDP4 cold shock gene sequences of Brassica rapa are obtained. It is shown that the isolated genes belong to a group AtCSP2/AtCSP4 of Arabidopsis thaliana and TsCSDP2/TsCSDP4 of Thellungiella salsuginea genes encoding proteins with a cold shock domain (CSD) and two zinc

miR398 and miR395 are involved in response to SO2 stress in Arabidopsis thaliana.

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Sulfur dioxide (SO2) is a common air pollutant that has adverse effects on plants. MicroRNAs (miRNAs) are small noncoding RNA that play critical roles in plant development and stress response. In this study, we found that two miRNAs, miR398 and miR395, were differentially expressed in Arabidopsis

Copper chaperone-dependent and -independent activation of three copper-zinc superoxide dismutase homologs localized in different cellular compartments in Arabidopsis.

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Superoxide dismutases (SODs) are important antioxidant enzymes that catalyze the disproportionation of superoxide anion to oxygen and hydrogen peroxide to guard cells against superoxide toxicity. The major pathway for activation of copper/zinc SOD (CSD) involves a copper chaperone for SOD (CCS) and

Different domains control the localization and mobility of LIKE HETEROCHROMATIN PROTEIN1 in Arabidopsis nuclei.

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Plants possess a single gene for the structurally related HETEROCHROMATIN PROTEIN1 (HP1), termed LIKE-HP1 (LHP1). We investigated the subnuclear localization, binding properties, and dynamics of LHP1 proteins in Arabidopsis thaliana cells. Transient expression assays showed that tomato (Solanum

miR398 regulation in rice of the responses to abiotic and biotic stresses depends on CSD1 and CSD2 expression

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MiR398 targets two Cu or Zn superoxide dismutases (CSD1 and CSD2) in Arabidopsis thaliana (L.) Heynh. Here we provide evidence that rice (Oryza sativa L.) miR398 mediates responses to abiotic and biotic stresses through regulating the expression of its target genes, Os-CSD1 and Os-CSD2. Rice plants

Overexpression of AtCSP4 affects late stages of embryo development in Arabidopsis.

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Eukaryotic cold shock domain proteins are nucleic acid-binding proteins that are involved in transcription, translation via RNA chaperone activity, RNA editing, and DNA repair during tissue developmental processes and stress responses. Cold shock domain proteins have been functionally implicated in

Arabidopsis cold shock domain protein 2 influences ABA accumulation in seed and negatively regulates germination.

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The cold shock domain (CSD) is the most conserved nucleic acid binding domain and is distributed from bacteria to animals and plants. CSD proteins are RNA chaperones that destabilize RNA secondary structures to regulate stress tolerance and development. AtCSP2 is one of the four CSD proteins in

Models for the mechanism for activating copper-zinc superoxide dismutase in the absence of the CCS Cu chaperone in Arabidopsis.

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Copper-zinc superoxide dismutase (CuZnSOD; CSD) is an important antioxidant enzyme for oxidative stress protection. To date, two activation pathways have been identified in many species. One requiring the CCS, Cu chaperone for SOD, to insert Cu and activate CSD (referred to as CCS-dependent

Arabidopsis COLD SHOCK DOMAIN PROTEIN 2 is a negative regulator of cold acclimation.

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Bacterial cold shock proteins (CSPs) act as RNA chaperones that destabilize mRNA secondary structures at low temperatures. Bacterial CSPs are composed solely of a nucleic acid-binding domain termed the cold shock domain (CSD). Plant CSD proteins contain an auxiliary domain in addition to the CSD but

Sucrose induction of Arabidopsis miR398 represses two Cu/Zn superoxide dismutases.

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MicroRNAs (miRNAs) are approximately 21-nt RNAs that reduce target accumulation through mRNA cleavage or translational repression. Arabidopsis miR398 regulates mRNAs encoding two copper superoxide dismutase (CSD) enzymes and a cytochrome c oxidase subunit. miR398 itself is down-regulated in response

Ambient temperature enhanced freezing tolerance of Chrysanthemum dichrum CdICE1 Arabidopsis via miR398.

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BACKGROUND ICE (Inducer of CBF Expression) family genes play an important role in the regulation of cold tolerance pathways. In an earlier study, we isolated the gene CdICE1 from Chrysanthemum dichrum and demonstrated that freezing tolerance was enhanced by CdICE1 overexpression. Therefore, we

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