Literature DB >> 32188942

Mass-spectrometry-based draft of the Arabidopsis proteome.

Julia Mergner1, Martin Frejno1, Markus List2, Michael Papacek3, Xia Chen4, Ajeet Chaudhary4, Patroklos Samaras1, Sandra Richter5, Hiromasa Shikata6,7, Maxim Messerer8, Daniel Lang8, Stefan Altmann9, Philipp Cyprys10, Daniel P Zolg1, Toby Mathieson11, Marcus Bantscheff11, Rashmi R Hazarika12,13, Tobias Schmidt1, Corinna Dawid14, Andreas Dunkel14, Thomas Hofmann14, Stefanie Sprunck10, Pascal Falter-Braun9,15, Frank Johannes12,13, Klaus F X Mayer8,16, Gerd Jürgens5, Mathias Wilhelm1, Jan Baumbach2, Erwin Grill3, Kay Schneitz4, Claus Schwechheimer6, Bernhard Kuster17,18,19.   

Abstract

Plants are essential for life and are extremely diverse organisms with unique molecular capabilities1. Here we present a quantitative atlas of the transcriptomes, proteomes and phosphoproteomes of 30 tissues of the model plant Arabidopsis thaliana. Our analysis provides initial answers to how many genes exist as proteins (more than 18,000), where they are expressed, in which approximate quantities (a dynamic range of more than six orders of magnitude) and to what extent they are phosphorylated (over 43,000 sites). We present examples of how the data may be used, such as to discover proteins that are translated from short open-reading frames, to uncover sequence motifs that are involved in the regulation of protein production, and to identify tissue-specific protein complexes or phosphorylation-mediated signalling events. Interactive access to this resource for the plant community is provided by the ProteomicsDB and ATHENA databases, which include powerful bioinformatics tools to explore and characterize Arabidopsis proteins, their modifications and interactions.

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Year:  2020        PMID: 32188942     DOI: 10.1038/s41586-020-2094-2

Source DB:  PubMed          Journal:  Nature        ISSN: 0028-0836            Impact factor:   49.962


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8.  PhosPhAt 4.0: An Updated Arabidopsis Database for Searching Phosphorylation Sites and Kinase-Target Interactions.

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9.  Plant Phosphopeptides Enrichment by Immobilized Metal Ion Affinity Chromatography.

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