Seeing the light with BLUF proteins

First described about 15 years ago, BLUF (Blue Light Using Flavin) domains are light-triggered switches that control enzyme activity or gene expression in response to blue light, remaining activated for seconds or even minutes after stimulation. The conserved, ferredoxin-like fold holds a flavin chr...

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Bibliographic Details
Published in:Biophysical reviews 2017-04, Vol.9 (2), p.169-176
Main Authors: Park, Sam-Yong, Tame, Jeremy R. H.
Format: Article
Language:English
Subjects:
Activation analysis
Atomic structure
Biochemistry
Biological and Medical Physics
Biological Techniques
Biomedical and Life Sciences
Biophysics
Cell Biology
Computer applications
Crystallography
Enzyme activity
Eukaryotes
Ferredoxin
Flavin
Gene expression
Genetics
Information processing
Life Sciences
Light
Membrane Biology
Nanotechnology
NMR
Nuclear magnetic resonance
Optics
Photon absorption
Prokaryotes
Proteins
Review
Spectroscopic analysis
Stimulation
Switches
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Summary:First described about 15 years ago, BLUF (Blue Light Using Flavin) domains are light-triggered switches that control enzyme activity or gene expression in response to blue light, remaining activated for seconds or even minutes after stimulation. The conserved, ferredoxin-like fold holds a flavin chromophore that captures the light and somehow triggers downstream events. BLUF proteins are found in both prokaryotes and eukaryotes and have a variety of architectures and oligomeric forms, but the BLUF domain itself seems to have a well-preserved structure and mechanism that have been the focus of intense study for a number of years. Crystallographic and NMR structures of BLUF domains have been solved, but the conflicting models have led to considerable debate about the atomic details of photo-activation. Advanced spectroscopic and computational methods have been used to analyse the early events after photon absorption, but these too have led to widely differing conclusions. New structural models are improving our understanding of the details of the mechanism and may lead to novel tailor-made tools for optogenetics.
ISSN:1867-2450
1867-2469
DOI:10.1007/s12551-017-0258-6