scholarly journals Alterations of Lysine Modifications on the Histone H3 N-Tail under Drought Stress Conditions in Arabidopsis thaliana

2009 ◽  
Vol 50 (10) ◽  
pp. 1856-1856 ◽  
Author(s):  
J.-M. Kim ◽  
T. K. To ◽  
J. Ishida ◽  
T. Morosawa ◽  
M. Kawashima ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Drought Stress ◽  
Histone H3 ◽  
Stress Conditions

scholarly journals Alterations of Lysine Modifications on the Histone H3 N-Tail under Drought Stress Conditions in Arabidopsis thaliana

2008 ◽  
Vol 49 (10) ◽  
pp. 1580-1588 ◽  
Author(s):  
Jong-Myong Kim ◽  
Taiko Kim To ◽  
Junko Ishida ◽  
Taeko Morosawa ◽  
Makiko Kawashima ◽  
...  
Keyword(s):  
Arabidopsis Thaliana ◽  
Drought Stress ◽  
Histone H3 ◽  
Stress Conditions

Flavonoid profiling by LC-MS IN 14 – 3-3ν knockout mutants of Arabidopsis thaliana during drought stress conditions

Planta Medica ◽  
2014 ◽  
Vol 80 (10) ◽  
Author(s):  
F Nabbie ◽  
O Shperdheja ◽  
J Millot ◽  
J Lindberg ◽  
B Peethambaran
Keyword(s):  
Arabidopsis Thaliana ◽  
Drought Stress ◽  
Stress Conditions ◽  
Knockout Mutants

scholarly journals F-box protein At1g08710 negatively regulates root length and imparts drought stress tolerance in Arabidopsis thaliana

2020 ◽  
Author(s):  
Venkateswara Rao ◽  
Virupapuram Vijaybhaskar
Keyword(s):  
Arabidopsis Thaliana ◽  
Drought Stress ◽  
Stress Tolerance ◽  
Stress Conditions ◽  
Stress Adaptation ◽  
List Type ◽  
E3 Ligases ◽  
Drought Stress Tolerance ◽  
Activator Protein ◽  
F Box Protein

AbstractPlants experience abiotic stresses throughout their life cycle and accordingly respond to tide over the unfavorable conditions. Drought or water deficit is one such condition to which plants respond in various ways including the ubiquitin proteasome system (UPS). Ubiquitin E3 ligases are a diverse family of protein complexes of which Skp1□Cullin□F□box (SCF) class mediate the ubiquitination and subsequent proteolytic turnover of proteins. F□box protein subunit plays crucial role in imparting specificity for selective degradation of target proteins. Here we report the function of Arabidopsis F-box protein At1g08710 in drought stress adaptation. As F-box protein is a constituent of SCF complex, here it is shown interacting with ASK1 and Cullin1. F-box protein localizes to both nucleus and membrane. F-box gene transcript accumulates highly in root and is altered in response to drought stress conditions. F-box protein interacts with a transcriptional co-activator protein ADA2b. F-box mutant plants displayed better growth under drought stress conditions compared to the wild type with a reduced accumulation of H2O2 and malondialdehyde (MDA). Drought responsive genes RD29A, RD22, ABI3 expression is also induced in F-box mutant plants. These results indicate F-box protein At1g08710 plays a role in drought stress adaptation in Arabidopsis thaliana.HighlightsF-box gene At1g08710 encodes a nuclear, membrane localized protein.F-box protein At1g08710 interacts with transcriptional co-activator protein ADA2b.F-box protein imparts drought stress tolerance by modulating H2O2 and MDA content.Drought response genes RD29A, RD22, ABI3 expression is induced in F-box mutant plants.

Tissue specificity of expression of heat shock gene ATHSP70-10 in Arabidopsis thaliana seedlings under normal and stress conditions

2020 ◽  
Vol 2020 (3) ◽  
pp. 37-47
Author(s):  
L.Ye. Kozeko ◽  
◽  
E.L. Kordyum ◽  
Keyword(s):  
Arabidopsis Thaliana ◽  
Heat Shock ◽  
Water Deficit ◽  
Tissue Specificity ◽  
Abiotic Factors ◽  
Root Apex ◽  
Stress Conditions ◽  
Heat Shock Gene ◽  
Organ Specificity ◽  
Pcr Analysis

Mitochondrial heat shock proteins of HSP70 family support protein homeostasis in mitochondria under normal and stress conditions. They provide folding and complex assembly of proteins encoded by mitochondrial genome, as well as import of cytosolic proteins to mitochondria, their folding and protection against aggregation. There are reports about organ-specificity of mitochondrial HSP70 synthesis in plants. However, tissue specificity of their functioning remains incompletely characterized. This problem was studied for mitochondrial AtHSP70-10 in Arabidopsis thaliana seedlings using a transgenic line with uidA signal gene under normal conditions, as well as high temperature and water deficit. Under normal conditions, histochemical GUS-staining revealed the expression of AtHSP70-10 in cotyledon and leaf hydathodes, stipules, central cylinder in root differentiation and mature zones, as well as weak staining in root apex and root-shoot junction zone. RT-PCR analysis of wild-type seedlings exposed to 37°C showed rapid upregulation of AtHSP70-10, which reached the highest level within 2 h. In addition, the gradual development of water deficit for 5 days caused an increase in transcription of this gene, which became more pronounced after 3 days and reached a maximum after 5 days of dehydration. Histochemical analysis showed complete preservation of tissue localization of AtHSP70-10 expression under both abiotic factors. The data obtained indicate the specific functioning of mitochondrial chaperone AtHSP70-10 in certain plant cellular structures.

scholarly journals Comparison of two Turnip mosaic virus P1 proteins in their ability to co-localize with the Arabidopsis thaliana G3BP-2 protein

Virus Genes ◽  
2021 ◽  
Vol 57 (2) ◽  
pp. 233-237
Author(s):  
Hendrik Reuper ◽  
Björn Krenz
Keyword(s):  
Arabidopsis Thaliana ◽  
Mosaic Virus ◽  
Specific Interaction ◽  
Viral Proteins ◽  
Turnip Mosaic Virus ◽  
Stress Conditions ◽  
C Terminus ◽  
Positive Sense ◽  
Key Factor ◽  
Large Host

AbstractTurnip mosaic virus (TuMV), belonging to the genus Potyvirus (family Potyviridae), has a large host range and consists of a single-stranded positive sense RNA genome encoding 12 proteins, including the P1 protease. This protein which is separated from the polyprotein by cis cleavage at its respective C-terminus, has been attributed with different functions during potyviral infection of plants. P1 of Turnip mosaic virus (P1-TuMV) harbors an FGSF-motif and FGSL-motif at its N-terminus. This motif is predicted to be a binding site for the host Ras GTPase-activating protein-binding protein (G3BP), which is a key factor for stress granule (SG) formation in mammalian systems and often targeted by viruses to inhibit SG formation. We therefore hypothesized that P1-TuMV might interact with G3BP to control and regulate plant SGs to optimize cellular conditions for the production of viral proteins. Here, we analyzed the co-localization of the Arabidopsis thaliana G3BP-2 with the P1 of two TuMV isolates, namely UK 1 and DEU 2. Surprisingly, P1-TuMV-DEU 2 co-localized with AtG3BP-2 under abiotic stress conditions, whereas P1-TuMV-UK 1 did not. AtG3BP-2::RFP showed strong SGs formation after stress, while P1-UK 1::eGFP maintained a chloroplastic signal under stress conditions, the signal of P1-DEU 2::eGFP co-localized with that of AtG3BP-2::RFP. This indicates a specific interaction between P1-DEU 2 and the AtG3BP family which is not solely based on the canonical interaction motifs.

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