Temperature variations have a big impact on bacterial metabolism and death, yet an exhaustive molecular picture of these processes is still missing. For instance, whether thermal death is determined by the deterioration of the whole or a specific part of the proteome is hotly debated. Here, by monitoring the proteome dynamics of E. coli, we clearly show that only a minor fraction of the proteome unfolds at the cell death. First, we prove that the dynamical state of the E. coli proteome is an excellent proxy for temperature-dependent bacterial metabolism and death. The proteome diffusive dynamics peaks at about the bacterial optimal growth temperature, then a dramatic dynamical slowdown is observed that starts just below the cell's death temperature. Next, we show that this slowdown is caused by the unfolding of just a small fraction of proteins that establish an entangling interprotein network, dominated by hydrophobic interactions, across the cytoplasm. Finally, the deduced progress of the proteome unfolding and its diffusive dynamics are both key to correctly reproduce the E. coli growth rate.

Institut de Biologie Physico Chimique Fondation Edmond de Rothschild 13 Rue Pierre et Marie Curie 75005Paris France

Institut Laue Langevin 38000Grenoble France

Institut Universitaire de France 75005Paris France

ISC CNR Dipartimento di Fisica Università Sapienza 00185Rome Italy

J Heyrovský Institute of Physical Chemistry Czech Academy of Sciences 182 23Prague 8 Czechia

Laboratoire de Biochimie Théorique CNRS Université de Paris Cité 13 Rue Pierre et Marie Curie 75005Paris France

Laboratoire de Bioénergétique et Ingénierie des Protéines BIP CNRS Aix Marseille Université 13400Marseille France

Lexma Technology1337 Massachusetts Avenue Arlington Massachusetts02476 United States

Università degli Studi di Perugia Dipartimento di Fisica e Geologia Via A Pascoli 06123Perugia PG Italy

Université Grenoble Alpes CNRS Laboratoire Interdisciplinaire de Physique 38400Saint Martin d'Héres France

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Evaluation of the relationship between color-tuning of photosynthetic excitons and thermodynamic stability of light-harvesting chromoproteins

Optimized OPEP Force Field for Simulation of Crowded Protein Solutions