Literature DB >> 24136529

Arabidopsis proteomics: a simple and standardizable workflow for quantitative proteome characterization.

Anja Rödiger1, Birgit Agne, Katja Baerenfaller, Sacha Baginsky.   

Abstract

Arabidopsis is the model plant of choice for large-scale proteome analyses, because its genome is well annotated, essentially free of sequencing errors, and relatively small with little redundancy. Furthermore, most Arabidopsis organs are susceptible to standard protein solubilization protocols making protein extraction relatively simple. Many different facets of functional plant proteomics were established with Arabidopsis such as mapping the subcellular proteomes of organelles, proteo-genomic peptide mapping, and numerous studies on the dynamic changes in protein modification and protein abundances. As most standard proteomics technologies are now routinely applied, research interest is increasingly shifting towards the reverse genetic characterization of gene function at the proteome level, i.e., by profiling the quantitative proteome of wild type in comparison with mutant plant tissue. We report here a simple, standardizable protocol for the large-scale comparative quantitative proteome characterization of different Arabidopsis organs based on normalized spectral counting and suggest a statistical framework for data interpretation. Based on existing organellar proteome maps, proteins can be assigned to organelles, thus allowing the identification of organelle-specific responses.

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Year:  2014        PMID: 24136529     DOI: 10.1007/978-1-62703-631-3_20

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  4 in total

1.  Visualization and dissemination of multidimensional proteomics data comparing protein abundance during Caenorhabditis elegans development.

Authors:  Michael Riffle; Gennifer E Merrihew; Daniel Jaschob; Vagisha Sharma; Trisha N Davis; William S Noble; Michael J MacCoss
Journal:  J Am Soc Mass Spectrom       Date:  2015-07-02       Impact factor: 3.109

2.  The RNA-binding protein RNP29 is an unusual Toc159 transport substrate.

Authors:  Julia Grimmer; Anja Rödiger; Wolfgang Hoehenwarter; Stefan Helm; Sacha Baginsky
Journal:  Front Plant Sci       Date:  2014-06-16       Impact factor: 5.753

3.  Exploring the Contribution of Autophagy to the Excess-Sucrose Response in Arabidopsis thaliana.

Authors:  Daniel Laloum; Sahar Magen; Yoram Soroka; Tamar Avin-Wittenberg
Journal:  Int J Mol Sci       Date:  2022-03-31       Impact factor: 5.923

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

Authors:  Lin Xi; Zhaoxia Zhang; Waltraud X Schulze
Journal:  Methods Mol Biol       Date:  2021
  4 in total

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