Biochemical and Genetic Interactions of Phospholipase D Alpha 1 and Mitogen-Activated Protein Kinase 3 Affect Arabidopsis Stress Response
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F19%3A73596872" target="_blank" >RIV/61989592:15310/19:73596872 - isvavai.cz</a>
Výsledek na webu
<a href="https://www.frontiersin.org/articles/10.3389/fpls.2019.00275/pdf" target="_blank" >https://www.frontiersin.org/articles/10.3389/fpls.2019.00275/pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3389/fpls.2019.00275" target="_blank" >10.3389/fpls.2019.00275</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Biochemical and Genetic Interactions of Phospholipase D Alpha 1 and Mitogen-Activated Protein Kinase 3 Affect Arabidopsis Stress Response
Popis výsledku v původním jazyce
Phospholipase D alpha 1 (PLD alpha 1, AT3G15730) and mitogen-activated protein kinases (MAPKs) participate on signaling-dependent events in plants. MAPKs are able to phosphorylate a wide range of substrates putatively including PLDs. Here we have focused on functional regulations of PLD alpha 1 by interactions with MAPKs, their colocalization and impact on salt stress and abscisic acid (ABA) tolerance in Arabidopsis. Yeast two-hybrid and bimolecular fluorescent assays showed that PLD alpha 1 interacts with MPK3. Immunoblotting analyses likewise confirmed connection between both these enzymes. Subcellularly we co-localized PLD alpha 1 with MPK3 in the cortical cytoplasm close to the plasma membrane and in cytoplasmic strands. Moreover, genetic interaction studies revealed that pld alpha 1mpk3 double mutant was resistant to a higher salinity and showed a higher tolerance to ABA during germination in comparison to single mutants and wild type. Thus, this study revealed importance of new biochemical and genetic interactions between PLD alpha 1 and MPK3 for Arabidopsis stress (salt and ABA) response.
Název v anglickém jazyce
Biochemical and Genetic Interactions of Phospholipase D Alpha 1 and Mitogen-Activated Protein Kinase 3 Affect Arabidopsis Stress Response
Popis výsledku anglicky
Phospholipase D alpha 1 (PLD alpha 1, AT3G15730) and mitogen-activated protein kinases (MAPKs) participate on signaling-dependent events in plants. MAPKs are able to phosphorylate a wide range of substrates putatively including PLDs. Here we have focused on functional regulations of PLD alpha 1 by interactions with MAPKs, their colocalization and impact on salt stress and abscisic acid (ABA) tolerance in Arabidopsis. Yeast two-hybrid and bimolecular fluorescent assays showed that PLD alpha 1 interacts with MPK3. Immunoblotting analyses likewise confirmed connection between both these enzymes. Subcellularly we co-localized PLD alpha 1 with MPK3 in the cortical cytoplasm close to the plasma membrane and in cytoplasmic strands. Moreover, genetic interaction studies revealed that pld alpha 1mpk3 double mutant was resistant to a higher salinity and showed a higher tolerance to ABA during germination in comparison to single mutants and wild type. Thus, this study revealed importance of new biochemical and genetic interactions between PLD alpha 1 and MPK3 for Arabidopsis stress (salt and ABA) response.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10611 - Plant sciences, botany
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Ostatní
Rok uplatnění
2019
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Frontiers in Plant Science
ISSN
1664-462X
e-ISSN
—
Svazek periodika
10
Číslo periodika v rámci svazku
MAR
Stát vydavatele periodika
CH - Švýcarská konfederace
Počet stran výsledku
15
Strana od-do
"275-1"-"275-15"
Kód UT WoS článku
000461542000001
EID výsledku v databázi Scopus
2-s2.0-85064217989