Cell-wide analysis of protein thermal unfolding reveals determinants of thermostability

Author:

Leuenberger Pascal12ORCID,Ganscha Stefan23,Kahraman Abdullah4ORCID,Cappelletti Valentina1,Boersema Paul J.1ORCID,von Mering Christian4ORCID,Claassen Manfred3,Picotti Paola1ORCID

Affiliation:

1. Institute of Biochemistry, Department of Biology, ETH Zurich (ETHZ), CH-8093 Zurich, Switzerland.

2. Systems Biology Graduate School PhD Program, ETHZ and University of Zurich, CH-8093 Zurich, Switzerland.

3. Institute of Molecular Systems Biology, Department of Biology, ETHZ, CH-8093 Zurich, Switzerland.

4. Institute of Molecular Life Sciences and Swiss Institute of Bioinformatics, University of Zurich, CH-8057 Zurich, Switzerland.

Abstract

How proteomes take the heat Living organisms are very sensitive to temperature, and much of this is attributed to its effect on the structure and function of proteins. Leuenberger et al. explored thermostability on a proteome-wide scale in bacteria, yeast, and human cells by using a combination of limited proteolysis and mass spectrometry (see the Perspective by Vogel). Their results suggest that temperature-induced cell death is caused by the loss of a subset of proteins with key functions. The study also provides insight into the molecular and evolutionary bases of protein and proteome stability. Science , this issue p. eaai7825 ; see also p. 794

Funder

European Research Council

Swiss National Science Foundation

Promedica Stiftung

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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