Eukaryotic phytochromes: Light-regulated serine/threonine protein kinases with histidine kinase ancestry
Eukaryotic phytochromes: Light-regulated serine/threonine protein kinases with histidine kinase ancestry
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DOI:
10.1073/pnas.95.23.13976
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发表时间:
1998-11-10
影响因子:
11.1
通讯作者:
Lagarias, JC
中科院分区:
文献类型:
--
作者:
Yeh, KC;Lagarias, JC
The discovery of cyanobacterial phytochrome histidine kinases, together with the evidence that phytochromes from higher plants display protein kinase activity, bind ATP analogs, and possess C-terminal domains similar to bacterial histidine kinases. has fueled the controversial hypothesis that the eukaryotic phytochrome family of photoreceptors are light-regulated enzymes. Here we demonstrate that purified recombinant phytochromes from a higher plant and a green alga exhibit serine/threonine kinase activity similar to that of phytochrome isolated from dark grown seedlings. Phosphorylation of recombinant oat phytochrome is a light- and chromophore-regulated intramolecular process. Eased on comparative protein sequence alignments and biochemical cross-talk experiments with the response regulator substrate of the cyanobacterial phytochrome Cph1, we propose that eukaryotic phytochromes are histidine kinase paralogs with serine/threonine specificity whose enzymatic activity diverged from that of a prokaryotic ancestor after duplication of the transmitter module.