Abstract
Many biological processes depend on the function of proteins that detect changes in a cell's environment and transmit the information to the cytoplasm, for example, peptide hormone receptors1. In Escherichia coli this class of proteins is exemplified by the sensory transducers (also called signalling proteins or methyl-accepting chemotaxis proteins) which have a central role in mediating chemotactic behaviour2,3. The sensory transducers are the products of four genes: tsr, tar, tap and trg. Each transducer detects changes in the environmental concentration of one or a very few attractants: Tsr, serine; Tar, aspartate and maltose; Tap, unknown; and Trg, ribose and galactose. Tsr and Tar act directly as chemoreceptors for the amino acid attractants4,5 and signal changes in their degree of occupancy to the flagellar apparatus. Detection of these changes in occupancy is made possible as the transducers are methylated at multiple glutamate residues6–9 such that their level of methylation reflects the most recent chemoeffector concentration. Biochemical10,11 and genetic12,13 information concerning the serine transducer protein has been accumulating rapidly but little is known about the structure of the molecule. We present here the nucleotide sequence of the tsr gene of E. coli; the amino acid sequence derived from it suggests that the Tsr transducer protein has a relatively simple transmembrane structure that may place limits on the mechanisms available for the transmission of sensory information into the cell.
This is a preview of subscription content, access via your institution
Access options
Subscribe to this journal
Receive 51 print issues and online access
$199.00 per year
only $3.90 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
Similar content being viewed by others
References
Rodbell, M. Nature 284, 17–22 (1980).
Springer, M. S., Goy, M. F. & Adler, J. Nature 264, 577–579 (1979).
Boyd, A. & Simon, M. A. Rev. Physiol. 44, 501–517 (1982).
Hedblom, M. L. & Adler, J. J. Bact. 144, 1048–1060 (1980).
Wang, E. A. & Koshland, D. E. Proc. natn. Acad. Sci. U.S.A. 77, 7157–7161 (1980).
Boyd, A. & Simon, M. J. Bact. 143, 809–815 (1980).
Chelsky, D. & Dahlquist, F. W. Proc. natn. Acad. Sci. U.S.A. 77, 2434–2438 (1980).
DeFranco, A. L. & Koshland, D. E. Proc. natn. Acad. Sci. U.S.A. 77, 2439–2443 (1980).
Engstrom, P. & Hazelbauer, G. L. Cell 20, 165–171 (1980).
Kehry, M. R. & Dahlquist, F. W. J. biol. Chem. 257, 10378–10386 (1982).
Kehry, M. R. & Dahlquist, F. W. Cell 29, 761–772 (1982).
Boyd, A., Krikos, A. & Simon, M. Cell 26, 333–343 (1981).
Parkinson, J. S., Slocum, M. K., Callahan, A. M., Sherris, D. & Houts, S. E. in Mobility and Recognition in Cell Biology (eds Sund, H. & Veeger, C.) (de Gruyter, New York, in the press).
Shine, J. & Dalgarno, J. Proc. natn. Acad. Sci. U.S.A. 71, 7342–7346 (1974).
Platt, T. Cell 24, 10–23 (1981).
Segrest, J. P. & Feldman, R. J. J. molec. Biol 87, 853–858 (1974).
Emr, S. D., Hall, M. N. & Silhavy, T. J. J. Cell Biol. 86, 701–711 (1980).
Dunn, R. et al. Proc. natn. Acad. Sci. U.S.A. 78, 6744–6748 (1981).
Buchel, D. E., Gronenborn, B. & Muller-Hill, B. Nature 283, 541–545 (1980).
Higgins, C. F. et al. Nature 298, 723–727 (1982).
Young, I. G., Rogers, B. L., Campbell, H. D., Jawarowski, A. & Dhaw, D. C. Eur. J. Biochem. 116, 165–170 (1981).
Engelman, D. N., Henderson, R., McLachlan, A. D. & Wallace, B. A. Proc. natn. Acad. Sci. U.S.A. 77, 2023–2027 (1980).
Kreil, G. A. Rev. Biochem. 50, 317–348 (1981).
Kehry, M. R., Dahlquist, F. W. & Bond, M. W. in Mobility and Recognition in Cell Biology (eds Sund, H. & Veeger, C.) (de Gruyter, New York, in the press).
Sherris, D. & Parkinson, J. S. Proc. natn. Acad. Sci. U.S.A. 78, 6051–6055 (1981).
Rollins, C. & Dahlquist, F. W. Cell 25, 333–340 (1981).
Chelsky, D. & Dahlquist, F. W. Biochemistry 19, 4633–4639 (1980).
Auerswald, E.-A., Ludwig, G. & Schaller, H. Cold Spring Harb. Symp. quant. Biol. 45, 107–113 (1981).
Smith, H. O. & Birnstiel, M. Nucleic Acids Res. 3, 2387–2398 (1981).
Maxam, A. & Gilbert, W. Meth. Enzym. 65, 499–560 (1980).
Sanger, F., Nicklen, S. & Coulson, A. R. Proc. natn. Acad. Sci. U.S.A. 74, 5463–5467 (1977).
Messing, J., Crea, R. & Seeburg, P. H. Nucleic Acids Res. 9, 309–321 (1981).
Staden, R. Nucleic Acids Res. 8, 3673–3694 (1980).
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Boyd, A., Kendall, K. & Simon, M. Structure of the serine chemoreceptor in Escherichia coli. Nature 301, 623–626 (1983). https://doi.org/10.1038/301623a0
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1038/301623a0
This article is cited by
-
Myoglobin-like aerotaxis transducers in Archaea and Bacteria
Nature (2000)
-
The dcr gene family of Desulfovibrio: Implications from the sequence of dcrH and phylogenetic comparison with other mcp genes
Antonie van Leeuwenhoek (1996)
-
The Escherichia coli C homoprotocatechuate degradative operon: hpc gene order, direction of transcription and control of expression
Molecular and General Genetics MGG (1993)
-
Behavioral responses to chemical cues by bacteria
Journal of Chemical Ecology (1986)
Comments
By submitting a comment you agree to abide by our Terms and Community Guidelines. If you find something abusive or that does not comply with our terms or guidelines please flag it as inappropriate.
