Receptor‐like kinase activity in membranes of Arabidopsis thaliana
- 12 November 1993
- journal article
- Published by Wiley in FEBS Letters
- Vol. 333 (3) , 306-310
- https://doi.org/10.1016/0014-5793(93)80676-l
Abstract
A class of protein kinases in the plant Arabidopsis thaliana has been identified which has biochemical characteristics similar to those of the animal receptor protein kinases. These plant protein kinases are membrane‐associated, glycosylated, exhibit a preference for Mn2+ relative to Mg2+, and range from 115 to 135 kDa when identified by renaturation after protein blotting. Evidence is presented that the TMK1 protein, a receptor‐like protein kinase identified in Arabidopsis from its cloned gene, is also glycosylated in its native form, and shows a preference for Mn2+ over Mg2+ when assayed for kinase activity. All of the plant receptor‐like protein kinases identified phosphorylate only serine and threonine residues.Keywords
This publication has 21 references indexed in Scilit:
- Receptor‐like protein kinase genes of Arabidopsis thalianaThe Plant Journal, 1993
- The TMK1 gene from Arabidopsis codes for a protein with structural and biochemical characteristics of a receptor protein kinase.Plant Cell, 1992
- The S-locus receptor kinase gene in a self-incompatible Brassica napus line encodes a functional serine/threonine kinase.Plant Cell, 1992
- Expression cloning of the TGF-β type II receptor, a functional transmembrane serine/threonine kinaseCell, 1992
- Relationship of a putative receptor protein kinase from maize to the S-locus glycoproteins of BrassicaNature, 1990
- Signal transduction by receptors with tyrosine kinase activityPublished by Elsevier ,1990
- GROWTH FACTOR RECEPTOR TYROSINE KINASESAnnual Review of Biochemistry, 1988
- Self-phosphorylation of epidermal growth factor receptor: evidence for a model of intermolecular allosteric activationBiochemistry, 1987
- Purification of cell membrane glycoproteins by lectin affinity chromatographyBiochimica et Biophysica Acta (BBA) - Reviews on Biomembranes, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970