Structure of a Light-Activated LOV Protein Dimer That Regulates Transcription
Year: 2011
Type: article
Abstract: Light, oxygen, or voltage (LOV) protein domains are present in many signaling proteins in bacteria, archaea, protists, plants, and fungi. The LOV protein VIVID (VVD) of the filamentous fungus Neurospora crassa enables the organism to adapt to constant or increasing amounts of light and facilitates proper entrainment of circadian rhythms. Here, we determined the crystal structure of the fully light-adapted VVD dimer and reveal the mechanism by which light-driven conformational change alters the oligomeric state of the protein. Light-induced formation of a cysteinyl-flavin adduct generated a new hydrogen bond network that released the amino (N) terminus from the protein core and restructured an acceptor pocket for binding of the N terminus on the opposite subunit of the dimer. Substitution of residues critical for the switch between the monomeric and the dimeric states of the protein had profound effects on light adaptation in Neurospora. The mechanism of dimerization of VVD provides molecular details that explain how members of a large family of photoreceptors convert light responses to alterations in protein-protein interactions.
Source: Science Signaling
Institutions: Cornell University, Dartmouth College, Dartmouth Health
Language: English
Topic: Light effects on plants
Subfield: Plant Science
Domain: Life Sciences
Open Access status: green
Awards: TGF-Beta and Androgen Signaling During Prostate Regression, Functional Analysis and Systems Biology of Filamentous Fungi, G1367849499, Identification and Analysis of Circadian Clock-Controlled Genes, Genetic and Molecular Dissection of the Neurospora Clock, G4008756567, Training in Biotechnology: Emphasis in Protein Chemistry, G6898742010, Genetic and Molecular Dissection of the Neurospora Clock, Molecular Basis for Entrainment of Circadian Clocks, G8456989264
OpenAlex ID: W2110657196