title: Mutations in the NPH1 locus of Arabidopsis disrupt the perception of phototropic stimuli.
abstract: The phototropic response is an important component of seedling establishment in higher plants because it orients the young seedlings for maximal photosynthetic light capture. Despite their obvious importance, little is known about the mechanisms underlying the perception and transduction of the light signals that induce phototropic curvatures. Here, we report the isolation of eight mutants of Arabidopsis that lack or have severely impaired phototropic responses. These nph (for nonphototropic hypocotyl) mutants comprise four genetic loci: nph1, nph2, nph3, and nph4. Physiological and biochemical characterization of the nph1 allele series indicated that the NPH1 locus may encode the apoprotein for a dual-chromophoric or multichromophoric holoprotein photoreceptor capable of absorbing UV-A, blue, and green light and that this photoreceptor regulates all the phototropic responses of Arabidopsis. It appears that the NPH1 protein is most likely a 120-kD plasma membrane-associated phosphoprotein because all of the nph1 mutations negatively affected the abundance of this protein. In addition, the putative NPH1 photoreceptor protein is genetically and biochemically distinct from the HY4 protein, which most likely acts as a photoreceptor for blue light-mediated hypocotyl growth inhibition. Furthermore, the NPH1 and HY4 proteins are not functionally redundant because mutations in either gene alone affect only one physiological response but not the other, thus providing strong support for the hypothesis that more than one blue light photoreceptor is required for the normal growth and development of a seedling.
authors.affiliation: Department of Plant Biology, Carnegie Institution of Washington, Stanford, California 94305-1297, USA.
authors.forename: E
authors.initials: E
authors.lastname: Liscum
authors.forename: W R
authors.initials: WR
authors.lastname: Briggs
mesh_terms: D017360:Arabidopsis / Q000235:genetics* / Q000378:metabolism; D029681:Arabidopsis Proteins; D056931:Cryptochromes; D029721:Drosophila Proteins; D005136:Eye Proteins; D005420:Flavoproteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D018506:Gene Expression Regulation, Plant; D017343:Genes, Plant; D018522:Gravitropism / Q000235:genetics / Q000502:physiology; D008565:Membrane Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D009154:Mutation; D010641:Phenotype; D010750:Phosphoproteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D017956:Photoreceptor Cells, Invertebrate; D045322:Photosynthetic Reaction Center Complex Proteins / Q000235:genetics; D018524:Phototropism / Q000235:genetics*; D010940:Plant Proteins / Q000032:analysis / Q000235:genetics / Q000502:physiology; D017346:Protein Serine-Threonine Kinases; D043562:Receptors, G-Protein-Coupled; D012639:Seeds / Q000235:genetics / Q000502:physiology
chemical_list: D029681:Arabidopsis Proteins; C538962:CRY1 protein, Arabidopsis; D056931:Cryptochromes; D029721:Drosophila Proteins; D005136:Eye Proteins; D005420:Flavoproteins; D008565:Membrane Proteins; D010750:Phosphoproteins; D045322:Photosynthetic Reaction Center Complex Proteins; D010940:Plant Proteins; D043562:Receptors, G-Protein-Coupled; C119828:cry protein, Drosophila; C103646:NPH1 protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases