Proteomics

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Meltome Atlas - thermal proteome stability across the tree of life


ABSTRACT: We have developed a mass spectrometry-based approach that allowed us to quantitatively monitor protein stability across a broad range of temperatures at the proteome scale (meltome). We profiled the meltomes of several microorganisms and eukaryotic species including human, allowing to investigate the determinants of protein thermostability and survival in various environmental niches. Moreover, we will make Meltome Atlas a valuable, publicly available resource for the biological community to investigate their proteins of interest in the context of protein thermostbility.

INSTRUMENT(S): Orbitrap Fusion Lumos, Exactive Plus

ORGANISM(S): Thermus Thermophilus (strain Hb8 / Atcc 27634 / Dsm 579) Picrophilus Torridus Oleispira Antarctica Danio Rerio (zebrafish) (brachydanio Rerio) Caenorhabditis Elegans Saccharomyces Cerevisiae (baker's Yeast) Bacillus Subtilis Drosophila Melanogaster (fruit Fly) Homo Sapiens (human) Escherichia Coli Arabidopsis Thaliana (mouse-ear Cress) Geobacillus Stearothermophilus Mus Musculus (mouse)

TISSUE(S): Hepatocyte, Blood Plasma, Seminal Plasma, Liver, Cerebrospinal Fluid, Fibroblast Of Lung, Fibroblast, Saliva, Milk

SUBMITTER: Anna Jarzab  

LAB HEAD: Bernhard Kuster

PROVIDER: PXD011929 | Pride | 2020-04-29

REPOSITORIES: Pride

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Publications


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 re  ...[more]

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