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- W2898867152 abstract "Biological processes consist of several consecutive and interacting steps as, for example, in signal transduction cascades or metabolic reaction chains. These processes are regulated by protein-protein interactions and the formation of larger protein complexes, which also occur within biological membranes. To gain a large-scale overview of complex-forming proteins and the composition of such complexes within the cellular membranes of Arabidopsis roots, we use the combination of size-exclusion chromatography and mass spectrometry. First, we identified complex-forming proteins by a retention shift analysis relative to expected retention times of monomeric proteins during size-exclusion chromatography. In a second step we predicted complex composition through pairwise correlation of elution profiles. As result we present an interactome of 963 proteins within cellular membranes of Arabidopsis roots. Identification of complex-forming proteins was highly robust between two independently grown root proteomes. The protein complex composition derived from pairwise correlations of coeluting proteins reproducibly identified stable protein complexes (ribosomes, proteasome, mitochondrial respiratory chain supercomplexes) but showed higher variance between replicates regarding transient interactions (e.g., interactions with kinases) within membrane protein complexes." @default.
- W2898867152 created "2018-11-09" @default.
- W2898867152 creator A5081359523 @default.
- W2898867152 creator A5090816444 @default.
- W2898867152 date "2018-11-13" @default.
- W2898867152 modified "2023-09-24" @default.
- W2898867152 title "Global Identification of Protein Complexes within the Membrane Proteome of Arabidopsis Roots Using a SEC-MS Approach" @default.
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- W2898867152 doi "https://doi.org/10.1021/acs.jproteome.8b00382" @default.
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- W2898867152 hasPublicationYear "2018" @default.
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