Analysis of a Receptor-Like Protein Kinase of Arabidopsis Thaliana

  • G. Eric Schaller
  • Sara Patterson
  • Anthony B. Bleecker


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.


Extracellular Domain Kinase Domain Maltose Binding Protein Leucine Rich Repeat Domain Receptor Protein Kinase 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • G. Eric Schaller
    • 1
  • Sara Patterson
    • 1
  • Anthony B. Bleecker
    • 1
  1. 1.Department of BotanyUniversity of WisconsinMadisonUSA

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