Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum

Herman E, Sachse M, Kroth PG, Kottke T (2013)
Biochemistry 52(18): 3094-3101.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ;
Abstract
Aureochromes have recently been shown to act as blue-light-regulated transcription factors in the stramenopile alga Vaucheria frigida. They comprise a light-, oxygen-, or voltage-sensitive (LOV) domain as a sensory module with flavin mononucleotide (FMN) as a chromophore and a basic region leucine zipper (bZIP) domain as an effector. Aureochromes are the only members of a large LOV protein family, where the effector domain is located N-terminal to the sensor domain. This domain inversion positions the linking J alpha helix of other LOV proteins to the terminus, raising the question of the role of J alpha in aureochrome signaling. In phototropins, signaling proceeds from LOV2 via dissociation and unwinding of the J alpha helix to the C-terminal kinase effector domain. In contrast, other LOV proteins have been demonstrated to activate the effector without the unfolding of J alpha. We investigated the LOV domain of aureochrome la from the diatom Phaeodactylum tricornutum both with and without the J alpha helix. Fourier transform infrared difference spectroscopy provides evidence that the J alpha helix unfolds upon illumination. This unfolding is prerequisite for light-induced dimerization of LOV. Under illumination, full conversion to the dimer was observed by size exclusion chromatography. In the absence of the helix, a monomer was detected in the dark and in the light. As a further effect, the recovery of the dark state is 6-fold slower in LOV-J alpha than LOV. We therefore postulate that the J alpha helix plays an important role in aureochrome signaling.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Herman E, Sachse M, Kroth PG, Kottke T. Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum. Biochemistry. 2013;52(18):3094-3101.
Herman, E., Sachse, M., Kroth, P. G., & Kottke, T. (2013). Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum. Biochemistry, 52(18), 3094-3101.
Herman, E., Sachse, M., Kroth, P. G., and Kottke, T. (2013). Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum. Biochemistry 52, 3094-3101.
Herman, E., et al., 2013. Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum. Biochemistry, 52(18), p 3094-3101.
E. Herman, et al., “Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum”, Biochemistry, vol. 52, 2013, pp. 3094-3101.
Herman, E., Sachse, M., Kroth, P.G., Kottke, T.: Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum. Biochemistry. 52, 3094-3101 (2013).
Herman, Elena, Sachse, Matthias, Kroth, Peter G., and Kottke, Tilman. “Blue-Light-Induced Unfolding of the J alpha Helix Allows for the Dimerization of Aureochrome-LOV from the Diatom Phaeodactylum tricornutum”. Biochemistry 52.18 (2013): 3094-3101.
This data publication is cited in the following publications:
This publication cites the following data publications:

9 Citations in Europe PMC

Data provided by Europe PubMed Central.

How can EPR spectroscopy help to unravel molecular mechanisms of flavin-dependent photoreceptors?
Nohr D, Rodriguez R, Weber S, Schleicher E., Front Mol Biosci 2(), 2015
PMID: 26389123
Photochemistry of flavoprotein light sensors.
Conrad KS, Manahan CC, Crane BR., Nat. Chem. Biol. 10(10), 2014
PMID: 25229449
Aureochrome 1 illuminated: structural changes of a transcription factor probed by molecular spectroscopy.
Kerruth S, Ataka K, Frey D, Schlichting I, Heberle J., PLoS ONE 9(7), 2014
PMID: 25058114
Blue light-induced dimerization of monomeric aureochrome-1 enhances its affinity for the target sequence.
Hisatomi O, Nakatani Y, Takeuchi K, Takahashi F, Kataoka H., J. Biol. Chem. 289(25), 2014
PMID: 24790107
A novel cryptochrome in the diatom Phaeodactylum tricornutum influences the regulation of light-harvesting protein levels.
Juhas M, von Zadow A, Spexard M, Schmidt M, Kottke T, Buchel C., FEBS J. 281(9), 2014
PMID: 24628952
Algal photoreceptors: in vivo functions and potential applications.
Kianianmomeni A, Hallmann A., Planta 239(1), 2014
PMID: 24081482
Aureochrome 1a is involved in the photoacclimation of the diatom Phaeodactylum tricornutum.
Schellenberger Costa B, Sachse M, Jungandreas A, Bartulos CR, Gruber A, Jakob T, Kroth PG, Wilhelm C., PLoS ONE 8(9), 2013
PMID: 24073211

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 23621750
PubMed | Europe PMC

Search this title in

Google Scholar