Trigger Factor and DnaK possess overlapping substrate pools and binding specificities.
Open accessAbstract
Summary: Ribosome‐associated Trigger Factor (TF) and the DnaK chaperone system assist the folding of newly synthesized proteins in Escherichia coli. Here, we show that DnaK and TF share a common substrate pool in vivo. In TF‐deficient cells, Δ tig, depleted for DnaK and DnaJ the amount of aggregated proteins increases with increasing temperature, amounting to 10% of total soluble protein (approximately 340 protein species) at 37°C. A similar population of proteins aggregated in DnaK depleted tig+ cells, albeit to a much lower extent. Ninety‐four aggregated proteins isolated from DnaK‐ and DnaJ‐depleted Δ tig cells were identified by mass spectrometry and found to include essential cytosolic proteins. Four potential in vivo substrates were screened for chaperone binding sites using peptide libraries. Although TF and DnaK recognize different binding motifs, 77% of TF binding peptides also associated with DnaK. In the case of the nascent polypeptides TF and DnaK competed for binding, however, with competitive advantage for TF. In vivo, the loss of TF is compensated by the induction of the heat shock response and thus enhanced levels of DnaK. In summary, our results demonstrate that the co‐operation of the two mechanistically distinct chaperones in protein folding is based on their overlap in substrate specificities.
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SecB is present in proteobacteria only and like TF is not essential; it forms a tetramer with surface-exposed hydrophobic areas involved in substrate binding.
“SecB is present in proteobacteria only and like TF not essential (Deuerling et al., 2003; Crane and Randall, 2017). It forms a tetramer with surface-exposed hydrophobic areas, which are involved in substrate binding (Knoblauch et al., 1999).”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Deuerling et al., 2003
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- Authors
- Deuerling, E., Patzelt, H., Vorderwülbecke, S., Rauch, T., Kramer, G., Schaffitzel, E., Mogk, A., Schulze‐Specking, A., Langen, H., & Bukau, B.
- Affiliations
- University of Freiburg (DE)
- Heidelberg University (DE)
- F. Hoffmann-La Roche AG (CH)
- Corresponding author
- Deuerling, Elke
- Bukau, Bernd
- Venue
- Molecular Microbiology
- Publisher
- Wiley
- Published
- 2003-02-19
- Volume
- 47
- Issue
- 5
- Pages
- 1317-1328
- ISSN
- 0950-382X (ISSN-L)
- 1365-2958
- OpenAlex
- W2170132114
- Cited by
- 203
- References
- 35
- Citations by year
- 2026: 2 · 2025: 7 · 2024: 5 · 2023: 4 · 2022: 3 · 2021: 19 · 2020: 5 · 2019: 7 · 2018: 7 · 2017: 10 · 2016: 9 · 2015: 5 · 2014: 16 · 2013: 7 · 2012: 10
- FWCI
- 5.97
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Molecular Microbiology (publishedVersion)
- PubMed (publishedVersion)
- KOPS (University of Konstanz) (submittedVersion, cc-by-nc-nd)
- FreiDok plus (Universitätsbibliothek Freiburg) (submittedVersion)
- Funders
- Boehringer Ingelheim Fonds
- Deutsche Forschungsgemeinschaft (SFB388)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Keywords
- precipitating factors, DnaK, molecular chaperones, protein folding, nascent polypeptide folding, protein aggregation, substrate specificity, Hsp40, heat shock response, Escherichia coli
- MeSH terms
- Heat-Shock Proteins, Protein Binding, Substrate Specificity, Protein Folding, Chaperonin 60, HSP70 Heat-Shock Proteins, Peptidylprolyl Isomerase, Protein Interaction Mapping, Escherichia coli Proteins, HSP40 Heat-Shock Proteins
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