Template-directed assembly of receptor signaling complexes
AssigneeUniversity of Massachusetts
InventorsRobert M. Weis, Anthony L. Shrout, David J. Montefusco
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AssigneeUniversity of Massachusetts
InventorsRobert M. Weis, Anthony L. Shrout, David J. Montefusco
Estimating the term…
Transmembrane receptors in the signaling pathways of bacterial chemotaxis systems influence cell motility by forming noncovalent complexes with the cytoplasmic signaling proteins to regulate their activity. The requirements for receptor-mediated activation of CheA, the principal kinase of the Escherichia coli chemotaxis signaling pathway, can be demonstrated using self-assembled clusters of a receptor fragment (CF) derived from the cytoplasmic domain of the aspartate receptor, Tar. Histidine-tagged Tar CF can be assembled on the surface of unilamellar vesicles via a lipid containing the Nickel-nitrilotriacetic acid moiety as a headgroup. The stability of such a complex can be controlled by the properties of the template including the size and composition, which can be used, for example, to vary the 2-dimensional concentration of receptor fragments. Surface-assembled CF is also found to serve as a substrate for receptor methylation, which is catalyzed by the receptor transferase. Since neither CheA activation nor CF methylation is observed in comparable samples in the absence of vesicles, it is concluded that surface-templating generates the organization among CF subunits required for biochemical activity.
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An in vitro assembly for use in protein assays, said assembly comprising:
A functional receptor complex, comprising:
An in vitro assembly for enhancing the function of a membrane-associated receptor protein component, said assembly comprising:
Dependencies are inferred from the claim text.