title: Light-induced Changes in the Dimerization Interface of Bacteriophytochromes.
abstract: Phytochromes are dimeric photoreceptor proteins that sense red light levels in plants, fungi, and bacteria. The proteins are structurally divided into a light-sensing photosensory module consisting of PAS, GAF, and PHY domains and a signaling output module, which in bacteriophytochromes typically is a histidine kinase (HK) domain. Existing structural data suggest that two dimerization interfaces exist between the GAF and HK domains, but their functional roles remain unclear. Using mutational, biochemical, and computational analyses of the Deinococcus radiodurans phytochrome, we demonstrate that two dimerization interfaces between sister GAF and HK domains stabilize the dimer with approximately equal contributions. The existence of both dimerization interfaces is critical for thermal reversion back to the resting state. We also find that a mutant in which the interactions between the GAF domains were removed monomerizes under red light. This implies that the interactions between the HK domains are significantly altered by photoconversion. The results suggest functional importance of the dimerization interfaces in bacteriophytochromes.
authors.affiliation: From the University of Gothenburg, Department of Chemistry and Molecular Biology, Gothenburg, SE-40530 Sweden and University of Jyvaskyla, Nanoscience Center, Department of Biological and Environmental Sciences, Jyväskylä, FI-40014 Finland.
authors.forename: Heikki
authors.initials: H
authors.lastname: Takala
authors.affiliation: From the University of Gothenburg, Department of Chemistry and Molecular Biology, Gothenburg, SE-40530 Sweden and.
authors.forename: Alexander
authors.initials: A
authors.lastname: Björling
authors.affiliation: University of Jyvaskyla, Nanoscience Center, Department of Biological and Environmental Sciences, Jyväskylä, FI-40014 Finland.
authors.forename: Marko
authors.initials: M
authors.lastname: Linna
authors.affiliation: From the University of Gothenburg, Department of Chemistry and Molecular Biology, Gothenburg, SE-40530 Sweden and westenho@chem.gu.se.
authors.forename: Sebastian
authors.initials: S
authors.lastname: Westenhoff
authors.affiliation: University of Jyvaskyla, Nanoscience Center, Department of Biological and Environmental Sciences, Jyväskylä, FI-40014 Finland janne.ihalainen@jyu.fi.
authors.forename: Janne A
authors.initials: JA
authors.lastname: Ihalainen
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D018360:Crystallography, X-Ray; D034301:Deinococcus / Q000737:chemistry / Q000201:enzymology / Q000378:metabolism* / Q000528:radiation effects*; D019281:Dimerization; D000071677:Histidine Kinase; D008027:Light; D010834:Phytochrome / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D011487:Protein Conformation / Q000528:radiation effects; D011494:Protein Kinases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D010834:Phytochrome; D011494:Protein Kinases; D000071677:Histidine Kinase
keywords: cell signaling; dimerization; high performance liquid chromatography (HPLC); histidine kinase; molecular dynamics; mutagenesis; photoreceptor; phytochrome; protein conformation; x-ray scattering