(1) Ethylene. A family of at least 5 proteins
appear to function as ethylene receptors in Arabidopsis. All five contain
a histidine kinase-like domain. In two of these proteins (ETR1 and ERS1)
there is complete conservation of the residues considered essential for
histidine kinase activity. Several of the ethylene receptors are hybrid
kinases, containing a response regulator-like domain in addition to the
histidine kinase-like domain.
(2) Cytokinin. Overexpression of the CKI1 protein in Arabidopsis results
in cytokinin-independent growth. CKI1 contains a histidine kinase domain
with the all the essential residues essential for activity. CKI1 is a
hybrid kinase.
(3) Red light/Phytochrome. Plant phytochromes contain histidine kinase-like
domains, but in all cases there is substantial divergence from the canonical
requirements for activity. Interestingly, in cyanobacteria, there is a
functional phytochrome histidine kinase and cognate response regulator.
(4) Pyruvate dehydrogenase. The pyruvate dehydrogenase of animal mitochondria has the features of a histidine kinase but appears to function as a serine kinase. Plant mitochondria and plastids contain a similar proteins.
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