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  DnaK Functions as a Central Hub in the E. coli Chaperone Network

Calloni, G., Chen, T., Schermann, S. M., Chang, H.-c., Genevaux, P., Agostini, F., et al. (2012). DnaK Functions as a Central Hub in the E. coli Chaperone Network. CELL REPORTS, 1(3), 251-264. doi:10.1016/j.celrep.2011.12.007.

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 Creators:
Calloni, Giulia1, Author              
Chen, Taotao1, Author              
Schermann, Sonya M.1, Author              
Chang, Hung-chun1, Author              
Genevaux, Pierre2, Author
Agostini, Federico2, Author
Gaetano Tartaglia, Gian2, Author
Hayer-Hartl, Manajit3, Author              
Hartl, F. Ulrich1, Author              
Affiliations:
1Hartl, Franz-Ulrich / Cellular Biochemistry, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565152              
2external, ou_persistent22              
3Hayer-Hartl, Manajit / Chaperonin-assisted Protein Folding, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565153              

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Free keywords: HSP70 MOLECULAR CHAPERONES; HEAT-SHOCK-PROTEIN; TRIGGER FACTOR; ESCHERICHIA-COLI; IN-VIVO; POLYPEPTIDE FLUX; GENE-EXPRESSION; CELL-CULTURE; AMINO-ACIDS; AGGREGATION
 Abstract: Cellular chaperone networks prevent potentially toxic protein aggregation and ensure proteome integrity. Here, we used Escherichia coli as a model to understand the organization of these networks, focusing on the cooperation of the DnaK system with the upstream chaperone Trigger factor (TF) and the downstream GroEL. Quantitative proteomics revealed that DnaK interacts with at least similar to 700 mostly cytosolic proteins, including similar to 180 relatively aggregation-prone proteins that utilize DnaK extensively during and after initial folding. Upon deletion of TF, DnaK interacts increasingly with ribosomal and other small, basic proteins, while its association with large multidomain proteins is reduced. DnaK also functions prominently in stabilizing proteins for subsequent folding by GroEL. These proteins accumulate on DnaK upon GroEL depletion and are then degraded, thus defining DnaK as a central organizer of the chaperone network. Combined loss of DnaK and TF causes proteostasis collapse with disruption of GroEL function, defective ribosomal biogenesis, and extensive aggregation of large proteins.

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Language(s): eng - English
 Dates: 2012-03
 Publication Status: Published in print
 Pages: 14
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: CELL REPORTS
Source Genre: Journal
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Publ. Info: 600 TECHNOLOGY SQUARE, 5TH FLOOR, CAMBRIDGE, MA 02139 USA : CELL PRESS
Pages: - Volume / Issue: 1 (3) Sequence Number: - Start / End Page: 251 - 264 Identifier: ISSN: 2211-1247