Document Detail


Crystal structures of Aureochrome1 LOV suggest new design strategies for optogenetics.
MedLine Citation:
PMID:  22483116     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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 β 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 Hβ 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:
Devrani Mitra; Xiaojing Yang; Keith Moffat
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2012-04-03
Journal Detail:
Title:  Structure (London, England : 1993)     Volume:  20     ISSN:  1878-4186     ISO Abbreviation:  Structure     Publication Date:  2012 Apr 
Date Detail:
Created Date:  2012-04-09     Completed Date:  2012-07-26     Revised Date:  2014-09-16    
Medline Journal Info:
Nlm Unique ID:  101087697     Medline TA:  Structure     Country:  United States    
Other Details:
Languages:  eng     Pagination:  698-706     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 Elsevier Ltd. All rights reserved.
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MeSH Terms
Descriptor/Qualifier:
Algal Proteins / chemistry*,  genetics,  metabolism
Binding Sites
Crystallography, X-Ray
Escherichia coli
Flavin Mononucleotide / chemistry*
Light
Light Signal Transduction / genetics
Models, Molecular
Photoreceptor Cells / chemistry*,  metabolism
Photosynthesis / genetics
Protein Binding
Protein Multimerization
Protein Structure, Quaternary
Protein Structure, Secondary
Protein Structure, Tertiary
Protein Subunits / chemistry,  genetics,  metabolism
Recombinant Proteins / chemistry,  genetics,  metabolism
Spectrometry, Fluorescence
Stramenopiles / chemistry*
Grant Support
ID/Acronym/Agency:
GM036452/GM/NIGMS NIH HHS; P41 RR007707/RR/NCRR NIH HHS; P41 RR007707-19/RR/NCRR NIH HHS; R01 GM036452/GM/NIGMS NIH HHS; R01 GM036452-27/GM/NIGMS NIH HHS; RR007707/RR/NCRR NIH HHS
Chemical
Reg. No./Substance:
0/Algal Proteins; 0/Protein Subunits; 0/Recombinant Proteins; 7N464URE7E/Flavin Mononucleotide
Comments/Corrections

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