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Published October 1992 | public
Journal Article

The TMK1 gene from Arabidopsis codes for a protein with structural and biochemical characteristics of a receptor protein kinase

Abstract

Genomic and cDNA clones that code for a protein with structural and biochemical properties similar to the receptor protein kinases from animals were obtained from Arabidopsis. Structural features of the predicted polypeptide include an amino-terminal membrane targeting signal sequence, a region containing blocks of leucine-rich repeat elements, a single putative membrane spanning domain, and a characteristic serine/threonine-specific protein kinase domain. The gene coding for this receptor-like transmembrane kinase was designated TMK1. Portions of the TMK1 gene were expressed in Escherichia coli, and antibodies were raised against the recombinant polypeptides. These antibodies immunodecorated a 120-kD polypeptide present in crude extracts and membrane preparations. The immunodetectable band was present in extracts from leaf, stem, root, and floral tissues. The kinase domain of TMK1 was expressed as a fusion protein in E. coli, and the purified fusion protein was found capable of autophosphorylation on serine and threonine residues. The possible role of the TMK1 gene product in transmembrane signaling is discussed.

Additional Information

© 1992 American Society of Plant Biologists. Received August 5, 1992; accepted August 20, 1992. Caren Chang and G. Eric Schaller contributed equally to this work. We thank Bill Eberhardt for help with the construction of expression plasmids. We thank the members of the Meyerowitz laboratory for their helpful comments on the manuscript. This work was supported by Department of Energy Grants No. DE-FG02-91ER20029.A000 (A.B.B.) and No. DE-FG03-88ER13873 (E.M.M.), and by National Science Foundation Fellowship No. DCB-8807636 (C.C.).

Additional details

Created:
August 20, 2023
Modified:
October 23, 2023