Proteomic and phosphoproteomic analyses of chromatin-associated proteins from Arabidopsis thaliana

Handle URI:
http://hdl.handle.net/10754/563629
Title:
Proteomic and phosphoproteomic analyses of chromatin-associated proteins from Arabidopsis thaliana
Authors:
Bigeard, Jean; Rayapuram, Naganand; Bonhomme, Ludovic; Hirt, Heribert ( 0000-0003-3119-9633 ) ; Pflieger, Delphine
Abstract:
The nucleus is the organelle where basically all DNA-related processes take place in eukaryotes, such as replication, transcription, and splicing as well as epigenetic regulation. The identification and description of the nuclear proteins is one of the requisites toward a comprehensive understanding of the biological functions accomplished in the nucleus. Many of the regulatory mechanisms of protein functions rely on their PTMs among which phosphorylation is probably one of the most important properties affecting enzymatic activity, interaction with other molecules, localization, or stability. So far, the nuclear and subnuclear proteome and phosphoproteome of the model plant Arabidopsis thaliana have been the subject of very few studies. In this work, we developed a purification protocol of Arabidopsis chromatin-associated proteins and performed proteomic and phosphoproteomic analyses identifying a total of 879 proteins of which 198 were phosphoproteins that were mainly involved in chromatin remodeling, transcriptional regulation, and RNA processing. From 230 precisely localized phosphorylation sites (phosphosites), 52 correspond to hitherto unidentified sites. This protocol and data thereby obtained should be a valuable resource for many domains of plant research.
KAUST Department:
Desert Agriculture Initiative; Biological and Environmental Sciences and Engineering (BESE) Division; Plant Science Program; Bioscience Program
Publisher:
Wiley-Blackwell
Journal:
PROTEOMICS
Issue Date:
10-Jul-2014
DOI:
10.1002/pmic.201400072
Type:
Article
ISSN:
16159853
Sponsors:
This work was supported by the Agence Nationale de la Recherche (ANR-2010-JCJC-1608 to D. P.) and by the King Abdullah University of Science and Technology. We thank Veronique Legros for technical assistance in MS.
Appears in Collections:
Articles; Bioscience Program; Plant Science Program; Desert Agriculture Initiative; Biological and Environmental Sciences and Engineering (BESE) Division

Full metadata record

DC FieldValue Language
dc.contributor.authorBigeard, Jeanen
dc.contributor.authorRayapuram, Nagananden
dc.contributor.authorBonhomme, Ludovicen
dc.contributor.authorHirt, Heriberten
dc.contributor.authorPflieger, Delphineen
dc.date.accessioned2015-08-03T12:04:54Zen
dc.date.available2015-08-03T12:04:54Zen
dc.date.issued2014-07-10en
dc.identifier.issn16159853en
dc.identifier.doi10.1002/pmic.201400072en
dc.identifier.urihttp://hdl.handle.net/10754/563629en
dc.description.abstractThe nucleus is the organelle where basically all DNA-related processes take place in eukaryotes, such as replication, transcription, and splicing as well as epigenetic regulation. The identification and description of the nuclear proteins is one of the requisites toward a comprehensive understanding of the biological functions accomplished in the nucleus. Many of the regulatory mechanisms of protein functions rely on their PTMs among which phosphorylation is probably one of the most important properties affecting enzymatic activity, interaction with other molecules, localization, or stability. So far, the nuclear and subnuclear proteome and phosphoproteome of the model plant Arabidopsis thaliana have been the subject of very few studies. In this work, we developed a purification protocol of Arabidopsis chromatin-associated proteins and performed proteomic and phosphoproteomic analyses identifying a total of 879 proteins of which 198 were phosphoproteins that were mainly involved in chromatin remodeling, transcriptional regulation, and RNA processing. From 230 precisely localized phosphorylation sites (phosphosites), 52 correspond to hitherto unidentified sites. This protocol and data thereby obtained should be a valuable resource for many domains of plant research.en
dc.description.sponsorshipThis work was supported by the Agence Nationale de la Recherche (ANR-2010-JCJC-1608 to D. P.) and by the King Abdullah University of Science and Technology. We thank Veronique Legros for technical assistance in MS.en
dc.publisherWiley-Blackwellen
dc.subjectArabidopsis thalianaen
dc.subjectChromatinen
dc.subjectNucleusen
dc.subjectPhosphoproteomicsen
dc.subjectPlant proteomicsen
dc.titleProteomic and phosphoproteomic analyses of chromatin-associated proteins from Arabidopsis thalianaen
dc.typeArticleen
dc.contributor.departmentDesert Agriculture Initiativeen
dc.contributor.departmentBiological and Environmental Sciences and Engineering (BESE) Divisionen
dc.contributor.departmentPlant Science Programen
dc.contributor.departmentBioscience Programen
dc.identifier.journalPROTEOMICSen
dc.contributor.institutionUnité de Recherche en Génomique Végétale (URGV); UMR INRA/CNRS/Université d?Evry Val d?Essonne/Saclay Plant Sciences; Evry Franceen
dc.contributor.institutionCNRS, UMR 8587; Evry Franceen
dc.contributor.institutionUniversité Evry Val d?Essonne (UEVE), LAMBE; Evry Franceen
kaust.authorRayapuram, Nagananden
kaust.authorHirt, Heriberten
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