Proteomic Analysis of Arabidopsis pld alpha 1 Mutants Revealed an Important Role of Phospholipase D Alpha 1 in Chloroplast Biogenesis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15310%2F19%3A73596877" target="_blank" >RIV/61989592:15310/19:73596877 - isvavai.cz</a>
Result on the web
<a href="https://www.frontiersin.org/articles/10.3389/fpls.2019.00089/pdf" target="_blank" >https://www.frontiersin.org/articles/10.3389/fpls.2019.00089/pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.3389/fpls.2019.00089" target="_blank" >10.3389/fpls.2019.00089</a>
Alternative languages
Result language
angličtina
Original language name
Proteomic Analysis of Arabidopsis pld alpha 1 Mutants Revealed an Important Role of Phospholipase D Alpha 1 in Chloroplast Biogenesis
Original language description
Phospholipase D alpha 1 (PLD alpha 1) is a phospholipid hydrolyzing enzyme playing multiple regulatory roles in stress responses of plants. Its signaling activity is mediated by phosphatidic acid (PA) production, capacity to bind, and modulate G-protein complexes or by interaction with other proteins. This work presents a quantitative proteomic analysis of two T-DNA insertion pld alpha 1 mutants of Arabidopsis thaliana. Remarkably, PLD alpha 1 knockouts caused differential regulation of many proteins forming protein complexes, while PLD alpha 1 might be required for their stability. Almost one third of differentially abundant proteins (DAPs) in pld alpha 1 mutants are implicated in metabolism and RNA binding. Latter functional class comprises proteins involved in translation, RNA editing, processing, stability, and decay. Many of these proteins, including those regulating chloroplast protein import and protein folding, share common functions in chloroplast biogenesis and leaf variegation. Consistently, pld alpha 1 mutants showed altered level of TIC40 (a major regulator of protein import into chloroplast), differential accumulation of photosynthetic protein complexes and changed chloroplast sizes as revealed by immunoblotting, blue-native electrophoresis, and microscopic analyses, respectively. Our proteomic analysis also revealed that genetic depletion of PLD alpha 1 also affected proteins involved in cell wall architecture, redox homeostasis, and abscisic acid signaling. Taking together, PLD alpha 1 appears as a protein integrating cytosolic and plastidic protein translations, plastid protein degradation, and protein import into chloroplast in order to regulate chloroplast biogenesis in Arabidopsis.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10611 - Plant sciences, botany
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Frontiers in Plant Science
ISSN
1664-462X
e-ISSN
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Volume of the periodical
10
Issue of the periodical within the volume
FEB
Country of publishing house
CH - SWITZERLAND
Number of pages
16
Pages from-to
"89-1"-"89-16"
UT code for WoS article
000458932400001
EID of the result in the Scopus database
2-s2.0-85064183775