IDEAS home Printed from https://ideas.repec.org/a/nat/natcom/v10y2019i1d10.1038_s41467-019-09107-y.html
   My bibliography  Save this article

Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP

Author

Listed:
  • Sindhuja Sridharan

    (Genome Biology Unit, European Molecular Biology Laboratory
    Cellzome, A GSK company)

  • Nils Kurzawa

    (Genome Biology Unit, European Molecular Biology Laboratory
    Candidate for joint PhD degree from EMBL and Heidelberg University, Faculty of Biosciences)

  • Thilo Werner

    (Cellzome, A GSK company)

  • Ina Günthner

    (Cellzome, A GSK company)

  • Dominic Helm

    (Proteomics Core Facility, European Molecular Biology Laboratory)

  • Wolfgang Huber

    (Genome Biology Unit, European Molecular Biology Laboratory)

  • Marcus Bantscheff

    (Cellzome, A GSK company)

  • Mikhail M. Savitski

    (Genome Biology Unit, European Molecular Biology Laboratory)

Abstract

Adenosine triphosphate (ATP) plays fundamental roles in cellular biochemistry and was recently discovered to function as a biological hydrotrope. Here, we use mass spectrometry to interrogate ATP-mediated regulation of protein thermal stability and protein solubility on a proteome-wide scale. Thermal proteome profiling reveals high affinity interactions of ATP as a substrate and as an allosteric modulator that has widespread influence on protein complexes and their stability. Further, we develop a strategy for proteome-wide solubility profiling, and discover ATP-dependent solubilization of at least 25% of the insoluble proteome. ATP increases the solubility of positively charged, intrinsically disordered proteins, and their susceptibility for solubilization varies depending on their localization to different membrane-less organelles. Moreover, a few proteins, exhibit an ATP-dependent decrease in solubility, likely reflecting polymer formation. Our data provides a proteome-wide, quantitative insight into how ATP influences protein structure and solubility across the spectrum of physiologically relevant concentrations.

Suggested Citation

  • Sindhuja Sridharan & Nils Kurzawa & Thilo Werner & Ina Günthner & Dominic Helm & Wolfgang Huber & Marcus Bantscheff & Mikhail M. Savitski, 2019. "Proteome-wide solubility and thermal stability profiling reveals distinct regulatory roles for ATP," Nature Communications, Nature, vol. 10(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09107-y
    DOI: 10.1038/s41467-019-09107-y
    as

    Download full text from publisher

    File URL: https://www.nature.com/articles/s41467-019-09107-y
    File Function: Abstract
    Download Restriction: no
    File URL: https://libkey.io/10.1038/s41467-019-09107-y?utm_source=ideas
    LibKey link: if access is restricted and if your library uses this service, LibKey will redirect you to where you can use your library subscription to access this item
    ---><---

    Citations

    Citations are extracted by the CitEc Project, subscribe to its RSS feed for this item.
    as


    Cited by:

    1. Cristina Sayago & Jana Sánchez-Wandelmer & Fernando García & Begoña Hurtado & Vanesa Lafarga & Patricia Prieto & Eduardo Zarzuela & Pilar Ximénez-Embún & Sagrario Ortega & Diego Megías & Oscar Fernánd, 2023. "Decoding protein methylation function with thermal stability analysis," Nature Communications, Nature, vol. 14(1), pages 1-18, December.
    2. Rene Yu-Hong Cheng & Joseph de Rutte & Cade Ellis K. Ito & Andee R. Ott & Lucie Bosler & Wei-Ying Kuo & Jesse Liang & Brian E. Hall & David J. Rawlings & Dino Di Carlo & Richard G. James, 2023. "SEC-seq: association of molecular signatures with antibody secretion in thousands of single human plasma cells," Nature Communications, Nature, vol. 14(1), pages 1-15, December.

    More about this item

    Statistics

    Access and download statistics

    Corrections

    All material on this site has been provided by the respective publishers and authors. You can help correct errors and omissions. When requesting a correction, please mention this item's handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-09107-y. See general information about how to correct material in RePEc.

    If you have authored this item and are not yet registered with RePEc, we encourage you to do it here. This allows to link your profile to this item. It also allows you to accept potential citations to this item that we are uncertain about.

    We have no bibliographic references for this item. You can help adding them by using this form .

    If you know of missing items citing this one, you can help us creating those links by adding the relevant references in the same way as above, for each refering item. If you are a registered author of this item, you may also want to check the "citations" tab in your RePEc Author Service profile, as there may be some citations waiting for confirmation.

    For technical questions regarding this item, or to correct its authors, title, abstract, bibliographic or download information, contact: Sonal Shukla or Springer Nature Abstracting and Indexing (email available below). General contact details of provider: http://www.nature.com .

    Please note that corrections may take a couple of weeks to filter through the various RePEc services.

    IDEAS is a RePEc service. RePEc uses bibliographic data supplied by the respective publishers.