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ClpS is an essential component of the N-end rule pathway in Escherichia coli

Author

Listed:
  • A. Erbse

    (Universität Heidelberg)

  • R. Schmidt

    (Universität Heidelberg)

  • T. Bornemann

    (Universität Heidelberg
    Universität Witten/Herdecke)

  • J. Schneider-Mergener

    (Universitätsklinikum Charite, Humboldt-Universität)

  • A. Mogk

    (Universität Heidelberg)

  • R. Zahn

    (Universität Heidelberg)

  • D. A. Dougan

    (Universität Heidelberg
    La Trobe University)

  • B. Bukau

    (Universität Heidelberg)

Abstract

The N-end rule states that the half-life of a protein is determined by the nature of its amino-terminal residue1. Eukaryotes and prokaryotes use N-terminal destabilizing residues as a signal to target proteins for degradation by the N-end rule pathway. In eukaryotes an E3 ligase, N-recognin, recognizes N-end rule substrates and mediates their ubiquitination and degradation by the proteasome1,2. In Escherichia coli, N-end rule substrates are degraded by the AAA + chaperone ClpA in complex with the ClpP peptidase (ClpAP)3. Little is known of the molecular mechanism by which N-end rule substrates are initially selected for proteolysis. Here we report that the ClpAP-specific adaptor, ClpS, is essential for degradation of N-end rule substrates by ClpAP in bacteria. ClpS binds directly to N-terminal destabilizing residues through its substrate-binding site distal to the ClpS–ClpA interface4, and targets these substrates to ClpAP for degradation. Degradation by the N-end rule pathway is more complex than anticipated and several other features are involved, including a net positive charge near the N terminus and an unstructured region between the N-terminal signal and the folded protein substrate. Through interaction with this signal, ClpS converts the ClpAP machine into a protease with exquisitely defined specificity, ideally suited to regulatory proteolysis.

Suggested Citation

  • A. Erbse & R. Schmidt & T. Bornemann & J. Schneider-Mergener & A. Mogk & R. Zahn & D. A. Dougan & B. Bukau, 2006. "ClpS is an essential component of the N-end rule pathway in Escherichia coli," Nature, Nature, vol. 439(7077), pages 753-756, February.
  • Handle: RePEc:nat:nature:v:439:y:2006:i:7077:d:10.1038_nature04412
    DOI: 10.1038/nature04412
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    1. Xin Lan & Wei Huang & Su Bin Kim & Dechen Fu & Thilini Abeywansha & Jiemin Lou & Udayakumaran Balamurugan & Yong Tae Kwon & Chang Hoon Ji & Derek J. Taylor & Yi Zhang, 2024. "Oligomerization and a distinct tRNA-binding loop are important regulators of human arginyl-transferase function," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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