Proteomic Analysis of Arabidopsis pld alpha 1 Mutants Revealed an Important Role of Phospholipase D Alpha 1 in Chloroplast Biogenesis

Kód výsledku v 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>

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

Proteomic Analysis of Arabidopsis pld alpha 1 Mutants Revealed an Important Role of Phospholipase D Alpha 1 in Chloroplast Biogenesis

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

Proteomic Analysis of Arabidopsis pld alpha 1 Mutants Revealed an Important Role of Phospholipase D Alpha 1 in Chloroplast Biogenesis

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10611 - Plant sciences, botany

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)

Rok uplatnění

2019

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Frontiers in Plant Science

ISSN

1664-462X

e-ISSN

—

Svazek periodika

10

Číslo periodika v rámci svazku

FEB

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

16

Strana od-do

"89-1"-"89-16"

Kód UT WoS článku

000458932400001

EID výsledku v databázi Scopus

2-s2.0-85064183775