Meltome atlas-thermal proteome stability across the tree of life

Anna Jarzab, Nils Kurzawa, Thomas Hopf, Matthias Moerch, Jana Zecha, Niels Leijten, Yangyang Bian, Eva Musiol, Melanie Maschberger, Gabriele Stoehr, Isabelle Becher, Charlotte Daly, Patroklos Samaras, Julia Mergner, Britta Spanier, Angel Angelov, Thilo Werner, Marcus Bantscheff, Mathias Wilhelm, Martin KlingensporSimone Lemeer, Wolfgang Liebl, Hannes Hahne*, Mikhail M Savitski*, Bernhard Kuster*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

Abstract

We have used a mass spectrometry-based proteomic approach to compile an atlas of the thermal stability of 48,000 proteins across 13 species ranging from archaea to humans and covering melting temperatures of 30-90 °C. Protein sequence, composition and size affect thermal stability in prokaryotes and eukaryotic proteins show a nonlinear relationship between the degree of disordered protein structure and thermal stability. The data indicate that evolutionary conservation of protein complexes is reflected by similar thermal stability of their proteins, and we show examples in which genomic alterations can affect thermal stability. Proteins of the respiratory chain were found to be very stable in many organisms, and human mitochondria showed close to normal respiration at 46 °C. We also noted cell-type-specific effects that can affect protein stability or the efficacy of drugs. This meltome atlas broadly defines the proteome amenable to thermal profiling in biology and drug discovery and can be explored online at http://meltomeatlas.proteomics.wzw.tum.de:5003/ and http://www.proteomicsdb.org.

Original languageEnglish
Pages (from-to)495-503
Number of pages9
JournalNature Methods
Volume17
Issue number5
DOIs
Publication statusPublished - May 2020

Keywords

  • Animals
  • Electron Transport Chain Complex Proteins/metabolism
  • Gene Expression Regulation
  • Humans
  • Mitochondria/metabolism
  • Prokaryotic Cells/metabolism
  • Protein Stability
  • Proteins/chemistry
  • Proteome/analysis
  • Software
  • Species Specificity
  • Transition Temperature

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