期刊
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
卷 108, 期 23, 页码 9449-9454出版社
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1100262108
关键词
allosteric regulation; photosensing; PER-ARNT-SIM domain
资金
- National Institutes of Health [R01 GM081875, R01 AI07000, T32 GM008297]
- National Science Foundation [0843662]
- Robert A. Welch Foundation [I-1424]
- University of California
- Gordon and Betty Moore Foundation
- Direct For Biological Sciences [0843662] Funding Source: National Science Foundation
- Div Of Molecular and Cellular Bioscience [0843662] Funding Source: National Science Foundation
Light-oxygen-voltage (LOV) domains are blue light-activated signaling modules integral to a wide range of photosensory proteins. Upon illumination, LOV domains form internal protein-flavin adducts that generate conformational changes which control effector function. Here we advance our understanding of LOV regulation with structural, biophysical, and biochemical studies of EL222, a light-regulated DNA-binding protein. The dark-state crystal structure reveals interactions between the EL222 LOV and helix-turnhelix domains that we show inhibit DNA binding. Solution biophysical data indicate that illumination breaks these interactions, freeing the LOV and helix-turn-helix domains of each other. This conformational change has a key functional effect, allowing EL222 to bind DNA in a light-dependent manner. Our data reveal a conserved signaling mechanism among diverse LOV-containing proteins, where light-induced conformational changes trigger activation via a conserved interaction surface.
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