The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Promiscuous Substrate Recognition in Folding and Assembly Activities of the Trigger Factor Chaperone
Open accessAbstract
SUMMARY Trigger factor (TF) is a molecular chaperone that famously binds to bacterial ribosomes where it contacts emerging nascent chains, but TF is also abundant free in the cytosol where its activity is less well characterized. In vitro studies show that TF promotes protein refolding. We find here that ribosome-free TF stably associates with and rescues from misfolding a large repertoire of full-length proteins. We identify over 170 members of this cytosolic Escherichia coli TF substrate proteome, including ribosomal protein S7. We analyzed the biochemical properties of a TF:S7 complex from Thermotoga maritima and determined its crystal structure. This is the first atomic-level structure of a promiscuous chaperone in complex with a physiological substrate protein. The structure of the complex reveals the molecular basis of substrate recognition by TF, indicates how TF could accelerate protein folding and suggests a role for TF in the biogenesis of protein complexes.
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Principles that Govern the Folding of Protein Chains
Anfinsen, C. B. (1973) · Science · doi:10.1126/science.181.4096.223 · Cited by 7,096
Interaction network containing conserved and essential protein complexes in Escherichia coli
Butland, G., Peregrín-Alvarez, J. M., Li, J., Yang, W., Yang, X., Canadien, V., Starostine, A., Richards, D., Beattie, B., Krogan, N., et al. (2005) · Nature · doi:10.1038/nature03239 · Cited by 1,201
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
Cited by
Protein export through the bacterial Sec pathway
Tsirigotaki, A., De Geyter, J., Šoštaric´, N., Economou, A., & Karamanou, S. (2017) · Nature Reviews Microbiology · doi:10.1038/nrmicro.2016.161 · Cited by 447
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
Chaperone networking facilitates protein targeting to the bacterial cytoplasmic membrane.
Castanié-Cornet, M.-P., Bruel, N., & Genevaux, P. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2013.11.007 · Cited by 129
Chaperone-Bound Clients: The Importance of Being Dynamic
Hiller, S. (2019) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2018.12.005 · Cited by 54
Peschke, M., Le Goff, M., Koningstein, G. M., Karyolaimos, A., de Gier, J.-W., van Ulsen, P., & Luirink, J. (2018) · Journal of Molecular Biology · doi:10.1016/j.jmb.2017.12.004 · Cited by 33
Metadata
- Authors
- Martinez-Hackert, E., & Hendrickson, W. A.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2009-09
- Volume
- 138
- Issue
- 5
- Pages
- 923-934
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2048945529
- Cited by
- 167
- References
- 3
- FWCI
- 4.92
- Type
- journal article
- Language
- en
- Open access
- bronze
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