| http://purl.uniprot.org/citations/30833950 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/30833950 | http://www.w3.org/2000/01/rdf-schema#comment | "Phospholipase D alpha 1 (PLDα1) 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 pldα1 mutants of Arabidopsis thaliana. Remarkably, PLDα1 knockouts caused differential regulation of many proteins forming protein complexes, while PLDα1 might be required for their stability. Almost one third of differentially abundant proteins (DAPs) in pldα1 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, pldα1 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 PLDα1 also affected proteins involved in cell wall architecture, redox homeostasis, and abscisic acid signaling. Taking together, PLDα1 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."xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.org/dc/terms/identifier | "doi:10.3389/fpls.2019.00089"xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/author | "Pechan T."xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/author | "Samaj J."xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/author | "Takac T."xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/author | "Samajova O."xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/date | "2019"xsd:gYear |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/name | "Front Plant Sci"xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/pages | "89"xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/title | "Proteomic Analysis of Arabidopsis pii>pldpi/i>alphapii>1pi/i> Mutants Revealed an Important Role of Phospholipase D Alpha 1 in Chloroplast Biogenesis."xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://purl.uniprot.org/core/volume | "10"xsd:string |
| http://purl.uniprot.org/citations/30833950 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/30833950 |
| http://purl.uniprot.org/citations/30833950 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/30833950 |
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| http://purl.uniprot.org/uniprot/#_Q84WM2-mappedCitation-30833950 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/30833950 |
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| http://purl.uniprot.org/uniprot/Q38882 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30833950 |
| http://purl.uniprot.org/uniprot/Q9FMD5 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30833950 |
| http://purl.uniprot.org/uniprot/Q84WM2 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/30833950 |