Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

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Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. / Carroni, Marta; Kummer, Eva; Oguchi, Yuki; Wendler, Petra; Clare, Daniel K; Sinning, Irmgard; Kopp, Jürgen; Mogk, Axel; Bukau, Bernd; Saibil, Helen R.

In: eLife, Vol. 3, 2014, p. e02481.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Carroni, M, Kummer, E, Oguchi, Y, Wendler, P, Clare, DK, Sinning, I, Kopp, J, Mogk, A, Bukau, B & Saibil, HR 2014, 'Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation', eLife, vol. 3, pp. e02481. https://doi.org/10.7554/eLife.02481

APA

Carroni, M., Kummer, E., Oguchi, Y., Wendler, P., Clare, D. K., Sinning, I., Kopp, J., Mogk, A., Bukau, B., & Saibil, H. R. (2014). Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. eLife, 3, e02481. https://doi.org/10.7554/eLife.02481

Vancouver

Carroni M, Kummer E, Oguchi Y, Wendler P, Clare DK, Sinning I et al. Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. eLife. 2014;3:e02481. https://doi.org/10.7554/eLife.02481

Author

Carroni, Marta ; Kummer, Eva ; Oguchi, Yuki ; Wendler, Petra ; Clare, Daniel K ; Sinning, Irmgard ; Kopp, Jürgen ; Mogk, Axel ; Bukau, Bernd ; Saibil, Helen R. / Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation. In: eLife. 2014 ; Vol. 3. pp. e02481.

Bibtex

@article{6f9b61e9b1ef409d876d9c7a9b9dbcbe,
title = "Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation",
abstract = "The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its mechanism of action are unclear. We obtained electron microscopy (EM) structures of the BAP variant of ClpB that binds the protease ClpP, clearly revealing MD density on the surface of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally oriented MDs form head-to-tail contacts and repress ClpB activity by preventing Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70 binding, and releasing the contact in adjacent subunits. Our data suggest a wavelike activation of ClpB subunits around the ring.DOI: http://dx.doi.org/10.7554/eLife.02481.001. ",
keywords = "Amino Acid Motifs, Cryoelectron Microscopy, Crystallography, X-Ray, Endopeptidase Clp, Escherichia coli/metabolism, Escherichia coli Proteins/chemistry, HSP70 Heat-Shock Proteins/metabolism, Heat-Shock Proteins/chemistry, Imaging, Three-Dimensional, Molecular Dynamics Simulation, Mutant Proteins/chemistry, Negative Staining, Protein Aggregates, Protein Binding, Protein Structure, Tertiary",
author = "Marta Carroni and Eva Kummer and Yuki Oguchi and Petra Wendler and Clare, {Daniel K} and Irmgard Sinning and J{\"u}rgen Kopp and Axel Mogk and Bernd Bukau and Saibil, {Helen R}",
note = "Copyright {\textcopyright} 2014, Carroni et al.",
year = "2014",
doi = "10.7554/eLife.02481",
language = "English",
volume = "3",
pages = "e02481",
journal = "eLife",
issn = "2050-084X",
publisher = "eLife Sciences Publications Ltd.",

}

RIS

TY - JOUR

T1 - Head-to-tail interactions of the coiled-coil domains regulate ClpB activity and cooperation with Hsp70 in protein disaggregation

AU - Carroni, Marta

AU - Kummer, Eva

AU - Oguchi, Yuki

AU - Wendler, Petra

AU - Clare, Daniel K

AU - Sinning, Irmgard

AU - Kopp, Jürgen

AU - Mogk, Axel

AU - Bukau, Bernd

AU - Saibil, Helen R

N1 - Copyright © 2014, Carroni et al.

PY - 2014

Y1 - 2014

N2 - The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its mechanism of action are unclear. We obtained electron microscopy (EM) structures of the BAP variant of ClpB that binds the protease ClpP, clearly revealing MD density on the surface of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally oriented MDs form head-to-tail contacts and repress ClpB activity by preventing Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70 binding, and releasing the contact in adjacent subunits. Our data suggest a wavelike activation of ClpB subunits around the ring.DOI: http://dx.doi.org/10.7554/eLife.02481.001.

AB - The hexameric AAA+ chaperone ClpB reactivates aggregated proteins in cooperation with the Hsp70 system. Essential for disaggregation, the ClpB middle domain (MD) is a coiled-coil propeller that binds Hsp70. Although the ClpB subunit structure is known, positioning of the MD in the hexamer and its mechanism of action are unclear. We obtained electron microscopy (EM) structures of the BAP variant of ClpB that binds the protease ClpP, clearly revealing MD density on the surface of the ClpB ring. Mutant analysis and asymmetric reconstructions show that MDs adopt diverse positions in a single ClpB hexamer. Adjacent, horizontally oriented MDs form head-to-tail contacts and repress ClpB activity by preventing Hsp70 interaction. Tilting of the MD breaks this contact, allowing Hsp70 binding, and releasing the contact in adjacent subunits. Our data suggest a wavelike activation of ClpB subunits around the ring.DOI: http://dx.doi.org/10.7554/eLife.02481.001.

KW - Amino Acid Motifs

KW - Cryoelectron Microscopy

KW - Crystallography, X-Ray

KW - Endopeptidase Clp

KW - Escherichia coli/metabolism

KW - Escherichia coli Proteins/chemistry

KW - HSP70 Heat-Shock Proteins/metabolism

KW - Heat-Shock Proteins/chemistry

KW - Imaging, Three-Dimensional

KW - Molecular Dynamics Simulation

KW - Mutant Proteins/chemistry

KW - Negative Staining

KW - Protein Aggregates

KW - Protein Binding

KW - Protein Structure, Tertiary

U2 - 10.7554/eLife.02481

DO - 10.7554/eLife.02481

M3 - Journal article

C2 - 24843029

VL - 3

SP - e02481

JO - eLife

JF - eLife

SN - 2050-084X

ER -

ID: 257864968