Abstract
The bacterial aspartate receptor was reconstructed to eliminate the transmembrane domain, thus connecting the recognition domain directly to the effector domain. The resulting soluble receptor folded correctly and was no longer an integral membrane protein. Upon aspartate binding, this soluble receptor was stabilized to a similar extent as that of the native receptor. Of interest, this soluble receptor retained the ability to signal from the recognition to the effector domain. This result defines more clearly the role of the membrane and transmembrane domains in signal transduction and suggests that some ligand-induced motions in receptor proteins do not require the membrane or transmembrane domain for information transmission.
References
46
Referenced
8
10.1073/pnas.74.11.4964
10.1073/pnas.74.2.533
10.1038/336139a0
- J B Stock, M G Surette Escherichia coli and Salmonella typhimurium: Cellular and Molecular BiologyF C Neidhardt, R I Curtiss, J L Ingraham, E C C Lin, K B Low, B Magansanik, W S Reznikoff, M Riley, M Schaechter, H E Umbarger, eds F C Neidhardt, R I Curtiss, J L Ingraham, E C C Lin, K B Low, B Magansanik, W S Reznikoff, M Riley, M Schaechter, H E Umbarger (Am. Soc. Microbiol, Washington DC) 1, 1103–1129 (1996). / Escherichia coli and Salmonella typhimurium: Cellular and Molecular Biology by Stock J B (1996)
10.1016/S0960-9822(02)00605-X
10.1016/0092-8674(95)90404-2
10.1016/S0021-9258(18)68781-2
10.1073/pnas.78.8.4791
10.1016/S0021-9258(19)69587-6
10.1073/pnas.78.2.1052
10.1038/324068a0
10.1073/pnas.86.15.5683
10.1016/0092-8674(87)90213-3
10.1016/0014-5793(92)80891-J
10.1021/bi00030a010
10.1074/jbc.270.41.24043
10.1073/pnas.93.6.2545
10.1021/bi00186a009
10.1126/science.2820061
10.1126/science.6302843
10.1073/pnas.85.18.6711
10.1073/pnas.85.1.83
10.1128/jb.135.1.45-53.1978
10.1021/bi00169a002
10.1111/j.1749-6632.1949.tb27297.x
- A V Hill J Physiol (London) 90, iv–vii (1910). / J Physiol (London) by Hill A V (1910)
10.1021/bi961481v
10.1016/0003-2697(76)90527-3
10.1073/pnas.82.15.4891
10.1016/S0021-9258(19)78090-9
10.1016/S0167-4838(96)00190-2
10.1126/science.1660187
- Chen X. & Koshland D. E. Jr. (1997) Biochemistry in press.
10.1006/jmbi.1995.0571
10.1126/science.271.5252.1113
10.1126/science.1661030
10.1126/science.274.5286.425
10.1126/science.274.5286.423
10.1111/j.1365-2958.1994.tb01312.x
10.1073/pnas.82.5.1326
10.1021/bi00178a001
10.1016/0092-8674(86)90779-8
10.1073/pnas.83.18.6930
10.1016/S0021-9258(18)54400-8
10.1016/0042-6822(87)90343-6
-
L P Fernando, R D LeClaire, S Obici, P J Zavodny, S W Russell, J L Pace J Immunol 147, 541–547 (1991).
(
10.4049/jimmunol.147.2.541
) / J Immunol by Fernando L P (1991)
Dates
Type | When |
---|---|
Created | 23 years, 1 month ago (July 26, 2002, 10:31 a.m.) |
Deposited | 2 years, 4 months ago (April 22, 2023, 8:07 a.m.) |
Indexed | 1 year, 3 months ago (May 12, 2024, 11:02 p.m.) |
Issued | 27 years, 10 months ago (Oct. 14, 1997) |
Published | 27 years, 10 months ago (Oct. 14, 1997) |
Published Online | 27 years, 10 months ago (Oct. 14, 1997) |
Published Print | 27 years, 10 months ago (Oct. 14, 1997) |
@article{Ottemann_1997, title={Converting a transmembrane receptor to a soluble receptor: Recognition domain to effector domain signaling after excision of the transmembrane domain}, volume={94}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.94.21.11201}, DOI={10.1073/pnas.94.21.11201}, number={21}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Ottemann, Karen M. and Koshland, Daniel E.}, year={1997}, month=oct, pages={11201–11204} }