<i>Arabidopsis</i> NPH1: A Protein Kinase with a Putative Redox-Sensing Domain
Eva Huala(Carnegie Institution for Science), Paul W. Oeller(Carnegie Institution for Science), Emmanuel Liscum(Carnegie Institution for Science), In‐Seob Han(Carnegie Institution for Science), Elise Larsen(Carnegie Institution for Science), Winslow R. Briggs(Carnegie Institution for Science)
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Abstract
The NPH1 (nonphototropic hypocotyl 1) gene encodes an essential component acting very early in the signal-transduction chain for phototropism. Arabidopsis NPH1 contains a serine-threonine kinase domain and LOV1 and LOV2 repeats that share similarity (36 to 56 percent) with Halobacterium salinarium Bat, Azotobacter vinelandii NIFL, Neurospora crassa White Collar-1, Escherichia coli Aer, and the Eag family of potassium-channel proteins from Drosophila and mammals. Sequence similarity with a known (NIFL) and a suspected (Aer) flavoprotein suggests that NPH1 LOV1 and LOV2 may be flavin-binding domains that regulate kinase activity in response to blue light-induced redox changes.
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