The DOI matches its Crossref record; 20 of the 20 references it cites were found in a registry or an index.
L23 protein functions as a chaperone docking site on the ribosome
Open accessAbstract
During translation, the first encounter of nascent polypeptides is with the ribosome-associated chaperones that assist the folding process—a principle that seems to be conserved in evolution. In Escherichia coli, the ribosome-bound Trigger Factor chaperones the folding of cytosolic proteins by interacting with nascent polypeptides. Here we identify a ribosome-binding motif in the amino-terminal domain of Trigger Factor. We also show the formation of crosslinked products between Trigger Factor and two adjacent ribosomal proteins, L23 and L29, which are located at the exit of the peptide tunnel in the ribosome. L23 is essential for the growth of E. coli and the association of Trigger Factor with the ribosome, whereas L29 is dispensable in both processes. Mutation of an exposed glutamate in L23 prevents Trigger Factor from interacting with ribosomes and nascent chains, and causes protein aggregation and conditional lethality in cells that lack the protein repair function of the DnaK chaperone. Purified L23 also interacts specifically with Trigger Factor in vitro. We conclude that essential L23 provides a chaperone docking site on ribosomes that directly links protein biosynthesis with chaperone-assisted protein folding.
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Cites
Thompson, J. D., Higgins, D. G., & Gibson, T. J. (1994) · Nucleic Acids Research · doi:10.1093/nar/22.22.4673 · Cited by 64,617
Experiments in molecular genetics
Miller, J. H. (1972) · Medical Entomology and Zoology · Cited by 27,157
One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products
Datsenko, K. A., & Wanner, B. L. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.120163297 · Cited by 14,782
Mass Spectrometric Sequencing of Proteins from Silver-Stained Polyacrylamide Gels
Shevchenko, A., Wilm, M., Vorm, O., & Mann, M. (1996) · Analytical Chemistry · doi:10.1021/ac950914h · Cited by 8,995
Nicholls, A., Sharp, K. A., & Honig, B. (1991) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.340110407 · Cited by 5,240
Molecular Chaperones in the Cytosol: from Nascent Chain to Folded Protein
Hartl, F. U., & Hayer-Hartl, M. (2002) · Science · doi:10.1126/science.1068408 · Cited by 3,347
The Complete Atomic Structure of the Large Ribosomal Subunit at 2.4 Å Resolution
Ban, N., Nissen, P., Hansen, J., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.905 · Cited by 3,327
Self-citationThe Structural Basis of Ribosome Activity in Peptide Bond Synthesis
Nissen, P., Hansen, J., Ban, N., Moore, P. B., & Steitz, T. A. (2000) · Science · doi:10.1126/science.289.5481.920 · Cited by 2,269
Self-citationFemtomole sequencing of proteins from polyacrylamide gels by nano-electrospray mass spectrometry
Wilm, M., Shevchenko, A., Houthaeve, T., Breit, S., Schweigerer, L., Fotsis, T., & Mann, M. (1996) · Nature · doi:10.1038/379466a0 · Cited by 1,680
Folding of Newly Translated Proteins In Vivo: The Role of Molecular Chaperones
Frydman, J. (2001) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.70.1.603 · Cited by 1,173
Cited by
Ferreira-Cerca, S., Pöll, G., Gleizes, P.-E., Tschochner, H., & Milkereit, P. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.09.005 · Cited by 309
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
Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.
Deuerling, E., Patzelt, H., Vorderwülbecke, S., Rauch, T., Kramer, G., Schaffitzel, E., Mogk, A., Schulze‐Specking, A., Langen, H., & Bukau, B. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03370.x · Cited by 203
Self-citationKudva, 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
Bornemann, T., Jöckel, J., Rodnina, M. V., & Wintermeyer, W. (2008) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1402 · Cited by 178
Metadata
- Authors
- Kramer, G., Rauch, T., Rist, W., Vorderwülbecke, S., Patzelt, H., Schulze-Specking, A., Ban, N., Deuerling, E., & Bukau, B.
- Venue
- Nature
- Published
- 2002-09
- Volume
- 419
- Issue
- 6903
- Pages
- 171-174
- ISSN
- 0028-0836 (ISSN-L)
- 1476-4687
- OpenAlex
- W2131907269
- Cited by
- 357
- References
- 20
- FWCI
- 9.18
- Type
- journal article
- Language
- en
- Open access
- green
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- Kramer, G., Rauch, T., Rist, W., Vorderwülbecke, S., Patzelt, H., Schulze-Specking, A., Ban, N., Deuerling, E., & Bukau, B. (2002). L23 protein functions as a chaperone docking site on the ribosome. Nature. https://doi.org/10.1038/nature01047
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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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