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

Bibliography:

Bigeard J, Rayapuram N, Bonhomme L, Heribert Hirt​, Pflieger D.​, Proteomic and phosphoproteomic analyses of chromatin-associated proteins from Arabidopsis thaliana.​ Proteomics. 2014 May 31. doi: 10.1002/pmic.201400072 PMID: 24889360

Authors:

Bigeard J, Rayapuram N, Bonhomme L, Heribert Hirt, Pflieger D.

Keywords:

Arabidopsis thaliana, Chromatin, Nucleus, Phosphoproteomics, Proteomics

Year:

2014

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 towards a comprehensive understanding of the biological functions accomplished in the nucleus. Many of the regulatory mechanisms of protein functions rely on their post-translational modifications amongst 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 were the objects 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.​ 

ISSN:

1615-9861