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Pervasive protein thermal stability variation during the cell cycle

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Item Type:Article
Title:Pervasive protein thermal stability variation during the cell cycle
Creators Name:Becher, I. and Andrés-Pons, A. and Romanov, N. and Stein, F. and Schramm, M. and Baudin, F. and Helm, D. and Kurzawa, N. and Mateus, A. and Mackmull, M.T. and Typas, A. and Müller, C.W. and Bork, P. and Beck, M. and Savitski, M.M.
Abstract:Quantitative mass spectrometry has established proteome-wide regulation of protein abundance and post-translational modifications in various biological processes. Here, we used quantitative mass spectrometry to systematically analyze the thermal stability and solubility of proteins on a proteome-wide scale during the eukaryotic cell cycle. We demonstrate pervasive variation of these biophysical parameters with most changes occurring in mitosis and G1. Various cellular pathways and components vary in thermal stability, such as cell-cycle factors, polymerases, and chromatin remodelers. We demonstrate that protein thermal stability serves as a proxy for enzyme activity, DNA binding, and complex formation in situ. Strikingly, a large cohort of intrinsically disordered and mitotically phosphorylated proteins is stabilized and solubilized in mitosis, suggesting a fundamental remodeling of the biophysical environment of the mitotic cell. Our data represent a rich resource for cell, structural, and systems biologists interested in proteome regulation during biological transitions.
Keywords:Thermal Proteome Profiling, Cell Cycle, Proteomics
Source:Cell
ISSN:0092-8674
Publisher:Cell Press (U.S.A.)
Volume:173
Number:6
Page Range:1495-1507
Date:31 May 2018
Official Publication:https://doi.org/10.1016/j.cell.2018.03.053
PubMed:View item in PubMed

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