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Site-directed cross-linking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis.
Open accessAbstract
Cysteine residues introduced at specific locations in the aspartate receptor of Salmonella typhimurium provide anchor points for cross-linking and serve as chemical markers for structural studies of this oligomeric receptor. These markers have been used to measure the rate of subunit exchange between oligomeric receptors and to show that ligand binding inhibits this exchange. The cysteine-containing receptors can be oxidatively cross-linked to completion within the oligomeric receptor, indicating that the receptor has an even number of subunits. Based on this observation, a technique has been developed that can be used to determine the oligomeric structure of proteins under a variety of experimental conditions. The technique involves the measurement of the effect of dilution by "cysteineless" receptor subunits on cross-linking and reveals that the aspartate receptor is dimeric in detergent solution, in a mixed-micelle system, and in reconstituted membrane vesicles. Binding of aspartate does not change the oligomeric structure of the receptor, indicating that transmembrane signaling occurs within an oligomeric receptor of constant size.
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Cites
Yarden, Y., & Schlessinger, J. (1987) · Biochemistry · doi:10.1021/bi00379a035 · Cited by 627
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Hazelbauer, G. L., Falke, J. J., & Parkinson, J. S. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.09.014 · Cited by 632
Milburn, M. V., Privé, G. G., Milligan, D. L., Scott, W. G., Yeh, J., Jancarik, J., Koshland, D. E., & Kim, S.-H. (1991) · Science · doi:10.1126/science.1660187 · Cited by 411
Self-citationCloning of a putative glutamate receptor: A low affinity kainate-binding subunit
Bettler, B., Egebjerg, J., Sharma, G., Pecht, G., Hermans-Borgmeyer, I., Moll, C., Stevens, C. F., & Heinemann, S. (1992) · Neuron · doi:10.1016/0896-6273(92)90292-l · Cited by 377
Gegner, J. A., Graham, D. R., Roth, A. F., & Dahlquist, F. W. (1992) · Cell · doi:10.1016/0092-8674(92)90247-a · Cited by 338
Metadata
- Authors
- Milligan, D. L., & Koshland, D. E.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1988-05
- Volume
- 263
- Issue
- 13
- Pages
- 6268-6275
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2101755633
- Cited by
- 232
- References
- 1
- FWCI
- 1.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Milligan, D. L., & Koshland, D. E. (1988). Site-directed cross-linking. Establishing the dimeric structure of the aspartate receptor of bacterial chemotaxis. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)68781-2
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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.