Abstract
Genomic and cDNA clones encoding a novel receptor-like protein kinase (TMK1) have been isolated from Arabidopsis thaliana. The predicted protein has an intracellular kinase domain most related to the receptor tyrosine kinases but containing diagnostic serine/threonine sequences, a transmembrane domain, and an extracellular domain containing 11 copies of a leucine rich repeat. Leucine rich repeats have only been found in proteins associated with the plasma membrane and are involved in protein/protein interactions. Domain-specific antibodies against the extracellular and intracellular domains of TMK1 have been made using fusion proteins expressed in E. coli. In extracts of Arabidopsis, the antibodies specifically immunodecorate a polypeptide of about 120 kD. The native TMK1 protein from Arabidopsis is capable of reversible binding to lectin columns, and digestion with endoglycosidase F reduces the apparent molecular mass of the immunodecorated protein by 10 kD, indicating that the native protein is glycosylated. The intracellular domain of TMK1 was expressed as a fusion protein with maltose binding protein in E. coli and was found capable of autophosphorylation on serine and threonine residues, indicating that the intracellular domain of TMK1 is a functional protein kinase.
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Schaller, G.E., Patterson, S., Bleecker, A.B. (1993). Analysis of a Receptor-Like Protein Kinase of Arabidopsis Thaliana . In: Amasino, R.M. (eds) Cellular Communication in Plants. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9607-0_19
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DOI: https://doi.org/10.1007/978-1-4757-9607-0_19
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