Structural basis for aggregate dissolution and refolding by the Mycobacterium tuberculosis ClpB-DnaK bi-chaperone system.


Journal

Cell reports
ISSN: 2211-1247
Titre abrégé: Cell Rep
Pays: United States
ID NLM: 101573691

Informations de publication

Date de publication:
25 05 2021
Historique:
received: 11 05 2020
revised: 30 12 2020
accepted: 03 05 2021
entrez: 26 5 2021
pubmed: 27 5 2021
medline: 11 2 2022
Statut: ppublish

Résumé

The M. tuberculosis (Mtb) ClpB is a protein disaggregase that helps to rejuvenate the bacterial cell. DnaK is a protein foldase that can function alone, but it can also bind to the ClpB hexamer to physically couple protein disaggregation with protein refolding, although the molecular mechanism is not well understood. Here, we report the cryo-EM analysis of the Mtb ClpB-DnaK bi-chaperone in the presence of ATPγS and a protein substrate. We observe three ClpB conformations in the presence of DnaK, identify a conserved TGIP loop linking the oligonucleotide/oligosaccharide-binding domain and the nucleotide-binding domain that is important for ClpB function, derive the interface between the regulatory middle domain of the ClpB and the DnaK nucleotide-binding domain, and find that DnaK binding stabilizes, but does not bend or tilt, the ClpB middle domain. We propose a model for the synergistic actions of aggregate dissolution and refolding by the Mtb ClpB-DnaK bi-chaperone system.

Identifiants

pubmed: 34038719
pii: S2211-1247(21)00508-8
doi: 10.1016/j.celrep.2021.109166
pmc: PMC8209680
mid: NIHMS1708604
pii:
doi:

Substances chimiques

Bacterial Proteins 0
Escherichia coli Proteins 0
Endopeptidase Clp EC 3.4.21.92

Types de publication

Journal Article Research Support, N.I.H., Extramural

Langues

eng

Sous-ensembles de citation

IM

Pagination

109166

Subventions

Organisme : NCI NIH HHS
ID : P30 CA008748
Pays : United States
Organisme : NIAID NIH HHS
ID : R01 AI070285
Pays : United States
Organisme : NIAID NIH HHS
ID : U19 AI111143
Pays : United States

Informations de copyright

Copyright © 2021 The Author(s). Published by Elsevier Inc. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests M.S.G. has received consulting fees and equity from Vedanta Biosciences and consulting fees from Takeda.

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Auteurs

Yanting Yin (Y)

Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Xiang Feng (X)

Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Hongjun Yu (H)

Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Allison Fay (A)

Immunology Program, Sloan Kettering Institute, New York, NY, USA.

Amanda Kovach (A)

Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA.

Michael S Glickman (MS)

Immunology Program, Sloan Kettering Institute, New York, NY, USA.

Huilin Li (H)

Department of Structural Biology, Van Andel Institute, Grand Rapids, MI, USA. Electronic address: huilin.li@vai.org.

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