1. Biochemistry and Chemical Biology
Download icon

Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms

Research Article
  • Cited 5
  • Views 1,017
  • Annotations
Cite this article as: eLife 2018;7:e34055 doi: 10.7554/eLife.34055

Abstract

Cdc48 is a AAA+ ATPase that plays an essential role for many cellular processes in eukaryotic cells. An archaeal homologue of this highly conserved enzyme was shown to directly interact with the 20S proteasome. Here, we analyze the occurrence and phylogeny of a Cdc48 homologue in Actinobacteria and assess its cellular function and possible interaction with the bacterial proteasome. Our data demonstrate that Cdc48-like protein of actinobacteria (Cpa) forms hexameric rings and that the oligomeric state correlates directly with the ATPase activity. Furthermore, we show that the assembled Cpa rings can physically interact with the 20S core particle. Comparison of the Mycobacterium smegmatis wild-type with a cpa knockout strain under carbon starvation uncovers significant changes in the levels of around 500 proteins. Pathway mapping of the observed pattern of changes identifies ribosomal proteins as a particular hotspot, pointing amongst others toward a role of Cpa in ribosome adaptation during starvation.

Article and author information

Author details

  1. Michal Ziemski

    Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland
    Competing interests
    The authors declare that no competing interests exist.
  2. Ahmad Jomaa

    Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland
    Competing interests
    The authors declare that no competing interests exist.
  3. Daniel Mayer

    Paul Scherrer Institute, Laboratory of Biomolecular Research, ETH Zurich, Zurich, Switzerland
    Competing interests
    The authors declare that no competing interests exist.
  4. Sonja Rutz

    Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland
    Competing interests
    The authors declare that no competing interests exist.
  5. Christoph Giese

    Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland
    Competing interests
    The authors declare that no competing interests exist.
  6. Dmitry Veprintsev

    Paul Scherrer Institute, Laboratory of Biomolecular Research, ETH Zurich, Zurich, Switzerland
    Competing interests
    The authors declare that no competing interests exist.
  7. Eilika Weber-Ban

    Institute of Molecular Biology and Biophysics, ETH Zurich, Zurich, Switzerland
    For correspondence
    eilika@mol.biol.ethz.ch
    Competing interests
    The authors declare that no competing interests exist.
    ORCID icon "This ORCID iD identifies the author of this article:" 0000-0002-5773-9274

Funding

Swiss National Science Foundation (163314)

  • Eilika Weber-Ban

The funders had no role in study design, data collection and interpretation, or the decision to submit the work for publication.

Reviewing Editor

  1. Andreas Martin, University of California, Berkeley, United States

Publication history

  1. Received: December 3, 2017
  2. Accepted: May 21, 2018
  3. Accepted Manuscript published: May 29, 2018 (version 1)
  4. Version of Record published: June 25, 2018 (version 2)

Copyright

© 2018, Ziemski et al.

This article is distributed under the terms of the Creative Commons Attribution License permitting unrestricted use and redistribution provided that the original author and source are credited.

Metrics

  • 1,017
    Page views
  • 226
    Downloads
  • 5
    Citations

Article citation count generated by polling the highest count across the following sources: Crossref, Scopus, PubMed Central.

Download links

A two-part list of links to download the article, or parts of the article, in various formats.

Downloads (link to download the article as PDF)

Download citations (links to download the citations from this article in formats compatible with various reference manager tools)

Open citations (links to open the citations from this article in various online reference manager services)

Further reading

    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics
    Andrea Graziadei et al.
    Research Article
    1. Biochemistry and Chemical Biology
    2. Structural Biology and Molecular Biophysics
    Xinru Wang et al.
    Research Article