The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
TatB and TatC Form a Functional and Structural Unit of the Twin-arginine Translocase from Escherichia coli
Open accessAbstract
In Escherichia coli, a subset of periplasmic proteins is exported via the twin-arginine translocation (Tat) pathway. In the present study, we have purified the Tat complex from E. coli, and we show that it contains only TatA, TatB, and TatC. Within the purified complex, TatB and TatC are present in a strict 1:1 ratio, suggesting a functional association. This has been confirmed by expression of a translational fusion between TatB and TatC. This Tat(BC) chimera supports efficient Tat-dependent export, indicating that TatB and TatC act as a unit in both structural and functional terms. The purified Tat complex contains varying levels of TatA, suggesting a gradual loss during isolation and a looser association. The molecular mass of the complex is approximately 600 kDa, demonstrating the presence of multiple copies of TatA, B, and C. Co-immunoprecipitation experiments show that TatC is required for the interaction of TatA with TatB, suggesting that TatA may interact with the complex via binding to TatC.
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Cites
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A common export pathway for proteins binding complex redox cofactors?
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Overlapping functions of components of a bacterial Sec-independent protein export pathway
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A Novel and Ubiquitous System for Membrane Targeting and Secretion of Cofactor-Containing Proteins
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A novel Sec-independent periplasmic protein translocation pathway in Escherichia coli
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Sec-independent Protein Translocation in Escherichia coli
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Cited by
The Bacterial Twin-Arginine Translocation Pathway
Lee, P. A., Tullman-Ercek, D., & Georgiou, G. (2006) · Annual Review of Microbiology · doi:10.1146/annurev.micro.60.080805.142212 · Cited by 347
Alami, M., Lüke, I., Deitermann, S., Eisner, G., Koch, H.-G., Brunner, J., & Müller, M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00398-8 · Cited by 317
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
- Bolhuis, A., Mathers, J. E., Thomas, J. D., Barrett, C. M. L., & Robinson, C.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2001-01
- Volume
- 276
- Issue
- 23
- Pages
- 20213-20219
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1985205346
- Cited by
- 260
- References
- 15
- FWCI
- 10.35
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Bolhuis, A., Mathers, J. E., Thomas, J. D., Barrett, C. M. L., & Robinson, C. (2001). TatB and TatC Form a Functional and Structural Unit of the Twin-arginine Translocase from Escherichia coli. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.m100682200
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
