Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain

Herman E, Kottke T (2015)
Biochemistry 54(7): 1484-1492.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Abstract / Bemerkung
Aureochromes have been shown to act as blue-light-regulated transcription factors in algae in the absence of phototropins. Aureochromes comprise a light-, oxygen-, or voltage-sensitive (LOV) domain as a sensory module binding the flavin chromophore and a basic region leucine zipper (bZIP) domain as an effector. The domain arrangement in aureochromes with an N-terminal effector is inversed to other LOV proteins. To clarify the role of the linking A'alpha helix in signaling, we have investigated the LOV domain of aureochrome1a from the diatom alga Phaeodactylum tricornutum without the N-terminal A'alpha helix but with the C-terminal Ja helix. Results were analyzed in comparison to those previously obtained on the LOV domain with both flanking helices and on the LOV domain with the A'alpha helix but without the Ja helix. Fourier transform infrared difference spectroscopy provides evidence by a band at 1656 cm(-1) that the A'alpha helix unfolds in response to light. This unfolding takes place only in the presence and as a consequence of the unfolding of the J alpha helix, which points to an allosteric regulation. Size exclusion chromatography shows the LOV domain to be dimeric in the absence and monomeric in the presence of the A'alpha helix, implying that the folded helix covers the dimerization site. Therefore, the A'alpha helix directly modulates the oligomerization state of the LOV domain, whereas the J alpha helix acts as an allosteric regulator. Both the allosteric control and the light-induced dimerization have not been observed in phototropin-LOV2 and point to a different signaling mechanism within the full-length proteins.
Erscheinungsjahr
Zeitschriftentitel
Biochemistry
Band
54
Zeitschriftennummer
7
Seite
1484-1492
ISSN
PUB-ID

Zitieren

Herman E, Kottke T. Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain. Biochemistry. 2015;54(7):1484-1492.
Herman, E., & Kottke, T. (2015). Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain. Biochemistry, 54(7), 1484-1492. doi:10.1021/bi501509z
Herman, E., and Kottke, T. (2015). Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain. Biochemistry 54, 1484-1492.
Herman, E., & Kottke, T., 2015. Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain. Biochemistry, 54(7), p 1484-1492.
E. Herman and T. Kottke, “Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain”, Biochemistry, vol. 54, 2015, pp. 1484-1492.
Herman, E., Kottke, T.: Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain. Biochemistry. 54, 1484-1492 (2015).
Herman, Elena, and Kottke, Tilman. “Allosterically Regulated Unfolding of the A'α Helix Exposes the Dimerization Site of the Blue-Light-Sensing Aureochrome-LOV Domain”. Biochemistry 54.7 (2015): 1484-1492.

10 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Functional characterization of a constitutively active kinase variant of Arabidopsis phototropin 1.
Petersen J, Inoue SI, Kelly SM, Sullivan S, Kinoshita T, Christie JM., J Biol Chem 292(33), 2017
PMID: 28663371
Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum.
Banerjee A, Herman E, Kottke T, Essen LO., Structure 24(1), 2016
PMID: 26688213
Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes.
Banerjee A, Herman E, Serif M, Maestre-Reyna M, Hepp S, Pokorny R, Kroth PG, Essen LO, Kottke T., Nucleic Acids Res 44(12), 2016
PMID: 27179025
Signaling States of a Short Blue-Light Photoreceptor Protein PpSB1-LOV Revealed from Crystal Structures and Solution NMR Spectroscopy.
Röllen K, Granzin J, Panwalkar V, Arinkin V, Rani R, Hartmann R, Krauss U, Jaeger KE, Willbold D, Batra-Safferling R., J Mol Biol 428(19), 2016
PMID: 27291287

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 25621532
PubMed | Europe PMC

Suchen in

Google Scholar