The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.
DnaK Functions as a Central Hub in the E. coli Chaperone Network
Open accessAbstract
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 ~700 mostly cytosolic proteins, including ~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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Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855
Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Ong, S.-E., Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., & Mann, M. (2002) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m200025-mcp200 · Cited by 5,574
From Levinthal to pathways to funnels
Dill, K. A., & Chan, H. S. (1997) · Nature Structural & Molecular Biology · doi:10.1038/nsb0197-10 · Cited by 2,293
Macromolecular crowding: an important but neglected aspect of the intracellular environment
Ellis, R. J. (2001) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00172-x · Cited by 1,153
Polypeptide Flux through Bacterial Hsp70
Teter, S. A., Houry, W. A., Ang, D., Tradler, T., Rockabrand, D., Fischer, G., Blum, P., Georgopoulos, C., & Hartl, F. U. (1999) · Cell · doi:10.1016/s0092-8674(00)80787-4 · Cited by 424
Self-citationHeidrich, C., Ursinus, A., Berger, J., Schwarz, H., & Höltje, J.-V. (2002) · Journal of Bacteriology · doi:10.1128/jb.184.22.6093-6099.2002 · Cited by 272
The native 3D organization of bacterial polysomes
Brandt, F., Etchells, S. A., Ortiz, J. O., Elcock, A. H., Hartl, F. U., & Baumeister, W. (2009) · Cell · doi:10.1016/j.cell.2008.11.016 · Cited by 258
Divergent stalling sequences sense and control cellular physiology.
Ito, K., Chiba, S., & Pogliano, K. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.01.073 · Cited by 107
Ligand crowding at a nascent signal sequence.
Eisner, G., Koch, H.-G., Beck, K., Brunner, J., & Müller, M. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200306069 · Cited by 69
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Shalgi, R., Hurt, J. A., Krykbaeva, I., Taipale, M., Lindquist, S., & Burge, C. B. (2013) · Molecular Cell · doi:10.1016/j.molcel.2012.11.028 · Cited by 339
Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones
Mayer, M. P., & Gierasch, L. M. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.rev118.002810 · Cited by 295
Structural basis for protein antiaggregation activity of the trigger factor chaperone.
Saio, T., Guan, X., Rossi, P., Economou, A., & Kalodimos, C. G. (2014) · Science · doi:10.1126/science.1250494 · Cited by 289
Evolution of heat‐shock protein expression underlying adaptive responses to environmental stress
Chen, B., Feder, M. E., & Kang, L. (2018) · Molecular Ecology · doi:10.1111/mec.14769 · Cited by 267
Kudva, R., Denks, K., Kuhn, P., Vogt, A., Müller, M., & Koch, H.-G. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.03.016 · Cited by 177
Metadata
- Authors
- Calloni, G., Chen, T., Schermann, S. M., Chang, H.-C., Genevaux, P., Agostini, F., Tartaglia, G. G., Hayer-Hartl, M., & Hartl, F. U.
- Venue
- Cell Reports
- Publisher
- Elsevier BV
- Published
- 2012-03
- Volume
- 1
- Issue
- 3
- Pages
- 251-264
- ISSN
- 2211-1247 (ISSN-L)
- OpenAlex
- W2172170548
- Cited by
- 380
- References
- 10
- FWCI
- 9.18
- Type
- journal article
- Language
- en
- Open access
- gold
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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