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Title: Crystal Structures of Aureochrome1 LOV Suggest New Design Strategies for Optogenetics

Aureochrome1, a signaling photoreceptor from a eukaryotic photosynthetic stramenopile, confers blue-light-regulated DNA binding on the organism. Its topology, in which a C-terminal LOV sensor domain is linked to an N-terminal DNA-binding bZIP effector domain, contrasts with the reverse sensor-effector topology in most other known LOV-photoreceptors. How, then, is signal transmitted in Aureochrome1? The dark- and light-state crystal structures of Aureochrome1 LOV domain (AuLOV) show that its helical N- and C-terminal flanking regions are packed against the external surface of the core {beta} sheet, opposite to the FMN chromophore on the internal surface. Light-induced conformational changes occur in the quaternary structure of the AuLOV dimer and in Phe298 of the H{beta} strand in the core. The properties of AuLOV extend the applicability of LOV domains as versatile design modules that permit fusion to effector domains via either the N- or C-termini to confer blue-light sensitivity.
Authors:
; ;  [1]
  1. (UC)
Publication Date:
OSTI Identifier:
1038286
Resource Type:
Journal Article
Resource Relation:
Journal Name: Structure; Journal Volume: 20; Journal Issue: (4) ; 04, 2012
Research Org:
Advanced Photon Source (APS), Argonne National Laboratory (ANL), Argonne, IL (US)
Sponsoring Org:
NIH
Country of Publication:
United States
Language:
ENGLISH
Subject:
59 BASIC BIOLOGICAL SCIENCES; 60 APPLIED LIFE SCIENCES; CONFORMATIONAL CHANGES; CRYSTAL STRUCTURE; DESIGN; DIMERS; DNA; SENSITIVITY; SENSORS; TOPOLOGY