Converting a transmembrane receptor to a soluble receptor: recognition domain to effector domain signaling after excision of the transmembrane domain.
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.
Ottemann
K M
KM
Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3206, USA.
Koshland
D E
DE
D001224:Aspartic Acid / Q000378:metabolism; D001665:Binding Sites; D002462:Cell Membrane / Q000378:metabolism / Q000648:ultrastructure; D002942:Circular Dichroism; D004926:Escherichia coli / Q000378:metabolism*; D008745:Methylation; D011487:Protein Conformation; D011489:Protein Denaturation; D017459:Receptors, Amino Acid / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D015398:Signal Transduction; D012995:Solubility; D013816:Thermodynamics
D017459:Receptors, Amino Acid; C031959:aspartic acid receptor; D001224:Aspartic Acid