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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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

  • 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