title: Phytochrome signaling: solving the Gordian knot with microbial relatives.
abstract: Phytochromes encompass a diverse collection of biliproteins that regulate numerous photoresponses in plants and microorganisms. Whereas the plant versions have proven experimentally intractable for structural studies, the microbial forms have recently provided important insights into how these photoreceptors work at the atomic level. Here, we review the current understanding of these microbial phytochromes, which shows that they have a modular dimeric architecture that propagates light-driven rotation of the bilin to distal contacts between adjacent signal output domains. Surprising features underpinning this signaling include: a deeply buried chromophore; a knot and hairpin loop that stabilizes the photosensing domain; and an extended helical spine that translates conformational changes in the photosensing domain to the output domain. Conservation within the superfamily both in modular construction and sequence strongly suggests that higher plant phytochromes work similarly as light-regulated toggle switches.
authors: Department of Genetics, 425-G Henry Mall, University of Wisconsin-Madison, Madison, WI 53706, USA. vierstra@wisc.edu
authors: Richard D
authors: RD
authors: Vierstra
authors: Junrui
authors: J
authors: Zhang
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry* / Q000502:physiology; D019281:Dimerization; D005656:Fungal Proteins / Q000737:chemistry* / Q000502:physiology; D008027:Light; D008958:Models, Molecular; D020283:Photoreceptors, Microbial / Q000737:chemistry / Q000528:radiation effects; D010834:Phytochrome / Q000737:chemistry* / Q000502:physiology; D017434:Protein Structure, Tertiary; D015398:Signal Transduction
chemical_list: D001426:Bacterial Proteins; D005656:Fungal Proteins; D020283:Photoreceptors, Microbial; D010834:Phytochrome