期刊
FEBS LETTERS
卷 585, 期 21, 页码 3391-3395出版社
WILEY
DOI: 10.1016/j.febslet.2011.10.003
关键词
Arabidopsis; Phototropin1; Kinase
资金
- Ministry of Education, Culture, Sports, Science and Technology (MEXT) of Japan [17084008, 22120005]
- Grants-in-Aid for Scientific Research [22120005, 17084008, 23657105] Funding Source: KAKEN
Phototropin is a blue light receptor in plants and is thought to be a light-regulated protein kinase. Previously, we defined the role of the photoreceptive domains, LOV1 and 2, in the light activation of the kinase in Arabidopsis phototropin2 (phot2) [1]. In this study, photoregulation of the kinase in phototropin1 (phot1) was studied using LOV2-linker-kinase polypeptide. We designed a new substrate consisting of the N-terminal part of the phot1 with autophosphorylation sites. The LOV2-linker-kinase had the same spectroscopic properties as those of the LOV2 core and phosphorylated the substrate in a light-dependent manner. Amino acid substitution experiments proved that the phosphorylation comes from the activation of the kinase via photoreaction of LOV2. Structured summary of protein interactions: AtPhot1-LOV2 phosphorylates AtPhot1-Nt by protein kinase assay (View Interaction: 1, 2, 3) (C) 2011 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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