Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Aggregation and Disaggregation Features of the Human Proteome

View ORCID ProfileTomi A Määttä, Mandy Rettel, Dominic Helm, View ORCID ProfileFrank Stein, View ORCID ProfileMikhail M Savitski
doi: https://doi.org/10.1101/2020.02.05.931675
Tomi A Määttä
1Genome Biology Unit, European Molecular Biology Laboratory, 69117, Heidelberg, Germany
2Collaboration for joint PhD degree between EMBL and Heidelberg University, Faculty of Biosciences
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Tomi A Määttä
Mandy Rettel
3Proteomics Core Facility, European Molecular Biology Laboratory, 69117, Heidelberg, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Dominic Helm
3Proteomics Core Facility, European Molecular Biology Laboratory, 69117, Heidelberg, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Frank Stein
3Proteomics Core Facility, European Molecular Biology Laboratory, 69117, Heidelberg, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Frank Stein
Mikhail M Savitski
1Genome Biology Unit, European Molecular Biology Laboratory, 69117, Heidelberg, Germany
3Proteomics Core Facility, European Molecular Biology Laboratory, 69117, Heidelberg, Germany
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Mikhail M Savitski
  • For correspondence: mikhail.savitski@embl.de
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Supplementary material
  • Preview PDF
Loading

ABSTRACT

Protein aggregates have negative implications in disease. While reductionist experiments have increased our understanding of aggregation processes, the systemic view in biological context is still limited. To extend this understanding, we used mass spectrometry-based proteomics to characterize aggregation and disaggregation in human cells after non-lethal heat shock. Aggregation-prone proteins were enriched in nuclear proteins, high proportion of intrinsically disordered regions, high molecular mass, high isoelectric point and hydrophilic amino acids. During recovery, most aggregating proteins disaggregated with a rate proportional to the aggregation propensity: larger loss in solubility was counteracted by faster disaggregation. High amount of intrinsically disordered regions also resulted in faster disaggregation. However, other characteristics enriched in aggregating proteins did not correlate with the disaggregation rates. In addition, we analyzed changes in protein thermal stability after heat shock. Soluble remnants of aggregated proteins were more thermally stable compared to control condition. Our results provide a rich resource of heat stress-related protein solubility data, propose novel roles for intrinsically disordered regions in protein quality control and reveal a protection mechanism to repress protein aggregation in heat stress.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
Back to top
PreviousNext
Posted February 05, 2020.
Download PDF

Supplementary Material

Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Aggregation and Disaggregation Features of the Human Proteome
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Aggregation and Disaggregation Features of the Human Proteome
Tomi A Määttä, Mandy Rettel, Dominic Helm, Frank Stein, Mikhail M Savitski
bioRxiv 2020.02.05.931675; doi: https://doi.org/10.1101/2020.02.05.931675
Digg logo Reddit logo Twitter logo Facebook logo Google logo LinkedIn logo Mendeley logo
Citation Tools
Aggregation and Disaggregation Features of the Human Proteome
Tomi A Määttä, Mandy Rettel, Dominic Helm, Frank Stein, Mikhail M Savitski
bioRxiv 2020.02.05.931675; doi: https://doi.org/10.1101/2020.02.05.931675

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Systems Biology
Subject Areas
All Articles
  • Animal Behavior and Cognition (3609)
  • Biochemistry (7585)
  • Bioengineering (5533)
  • Bioinformatics (20824)
  • Biophysics (10344)
  • Cancer Biology (7995)
  • Cell Biology (11653)
  • Clinical Trials (138)
  • Developmental Biology (6616)
  • Ecology (10224)
  • Epidemiology (2065)
  • Evolutionary Biology (13639)
  • Genetics (9556)
  • Genomics (12856)
  • Immunology (7929)
  • Microbiology (19568)
  • Molecular Biology (7675)
  • Neuroscience (42180)
  • Paleontology (308)
  • Pathology (1259)
  • Pharmacology and Toxicology (2208)
  • Physiology (3271)
  • Plant Biology (7057)
  • Scientific Communication and Education (1295)
  • Synthetic Biology (1953)
  • Systems Biology (5433)
  • Zoology (1119)