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 L-O, Kottke T (2016)
Nucleic Acids Research 44(12): 5957-5970.

Zeitschriftenaufsatz | Veröffentlicht | Englisch
 
Download
Es wurden keine Dateien hochgeladen. Nur Publikationsnachweis!
DOI
Autor*in
Banerjee, Ankan; Herman, ElenaUniBi; Serif, Manuel; Maestre-Reyna, Manuel; Hepp, Sebastian; Pokorny, Richard; Kroth, Peter G.; Essen, Lars-Oliver; Kottke, TilmanUniBi
Einrichtung
Fakultät für Chemie > Physikalische und Biophysikalische Chemie
Erscheinungsjahr
2016
Zeitschriftentitel
Nucleic Acids Research
Band
44
Ausgabe
12
Seite(n)
5957-5970
Urheberrecht / Lizenzen
Creative Commons Namensnennung-Nicht kommerziell 4.0 International (CC BY-NC 4.0)
ISSN
0305-1048, 1362-4962
Page URI
https://pub.uni-bielefeld.de/record/2905751

Zitieren

Banerjee A, Herman E, Serif M, et al. Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes. Nucleic Acids Research. 2016;44(12):5957-5970.
Banerjee, A., Herman, E., Serif, M., Maestre-Reyna, M., Hepp, S., Pokorny, R., Kroth, P. G., et al. (2016). Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes. Nucleic Acids Research, 44(12), 5957-5970. doi:10.1093/nar/gkw420
Banerjee, Ankan, Herman, Elena, Serif, Manuel, Maestre-Reyna, Manuel, Hepp, Sebastian, Pokorny, Richard, Kroth, Peter G., Essen, Lars-Oliver, and Kottke, Tilman. 2016. “Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes”. Nucleic Acids Research 44 (12): 5957-5970.
Banerjee, A., Herman, E., Serif, M., Maestre-Reyna, M., Hepp, S., Pokorny, R., Kroth, P. G., Essen, L. - O., and Kottke, T. (2016). Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes. Nucleic Acids Research 44, 5957-5970.
Banerjee, A., et al., 2016. Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes. Nucleic Acids Research, 44(12), p 5957-5970.
A. Banerjee, et al., “Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes”, Nucleic Acids Research, vol. 44, 2016, pp. 5957-5970.
Banerjee, A., Herman, E., Serif, M., Maestre-Reyna, M., Hepp, S., Pokorny, R., Kroth, P.G., Essen, L.-O., Kottke, T.: Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes. Nucleic Acids Research. 44, 5957-5970 (2016).
Banerjee, Ankan, Herman, Elena, Serif, Manuel, Maestre-Reyna, Manuel, Hepp, Sebastian, Pokorny, Richard, Kroth, Peter G., Essen, Lars-Oliver, and Kottke, Tilman. “Allosteric communication between DNA-binding and light-responsive domains of diatom class I aureochromes”. Nucleic Acids Research 44.12 (2016): 5957-5970.

6 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Arguments for an additional long-lived intermediate in the photocycle of the full-length aureochrome 1c receptor: A time-resolved small-angle X-ray scattering study.
Bannister S, Böhm E, Zinn T, Hellweg T, Kottke T., Struct Dyn 6(3), 2019
PMID: 31263739
bHLH-PAS protein RITMO1 regulates diel biological rhythms in the marine diatom Phaeodactylum tricornutum.
Annunziata R, Ritter A, Fortunato AE, Manzotti A, Cheminant-Navarro S, Agier N, Huysman MJJ, Winge P, Bones AM, Bouget FY, Cosentino Lagomarsino M, Bouly JP, Falciatore A., Proc Natl Acad Sci U S A 116(26), 2019
PMID: 31171659
Quantitative analyses of the equilibria among DNA complexes of a blue-light-regulated bZIP module, Photozipper.
Nakatani Y, Hisatomi O., Biophys Physicobiol 15(), 2018
PMID: 29450110
Algal light sensing and photoacclimation in aquatic environments.
Duanmu D, Rockwell NC, Lagarias JC., Plant Cell Environ 40(11), 2017
PMID: 28245058
PtAUREO1a and PtAUREO1b knockout mutants of the diatom Phaeodactylum tricornutum are blocked in photoacclimation to blue light.
Mann M, Serif M, Jakob T, Kroth PG, Wilhelm C., J Plant Physiol 217(), 2017
PMID: 28610707
The Influence of a Cryptochrome on the Gene Expression Profile in the Diatom Phaeodactylum tricornutum under Blue Light and in Darkness.
König S, Eisenhut M, Bräutigam A, Kurz S, Weber APM, Büchel C., Plant Cell Physiol 58(11), 2017
PMID: 29016997

57 References

Daten bereitgestellt von Europe PubMed Central.

Phototropin blue-light receptors.
Christie JM., Annu Rev Plant Biol 58(), 2007
PMID: 17067285
Higher plants use LOV to perceive blue light.
Demarsy E, Fankhauser C., Curr. Opin. Plant Biol. 12(1), 2008
PMID: 18930433
Function, structure and mechanism of bacterial photosensory LOV proteins.
Herrou J, Crosson S., Nat. Rev. Microbiol. 9(10), 2011
PMID: 21822294
From Plant Infectivity to Growth Patterns: The Role of Blue-Light Sensing in the Prokaryotic World.
Losi A, Mandalari C, Gartner W., Plants (Basel) 3(1), 2014
PMID: 27135492
VIVID is a flavoprotein and serves as a fungal blue light photoreceptor for photoadaptation.
Schwerdtfeger C, Linden H., EMBO J. 22(18), 2003
PMID: 12970196
Bacterial sensors of oxygen.
Green J, Crack JC, Thomson AJ, LeBrun NE., Curr. Opin. Microbiol. 12(2), 2009
PMID: 19246238
Photochemical and mutational analysis of the FMN-binding domains of the plant blue light receptor, phototropin.
Salomon M, Christie JM, Knieb E, Lempert U, Briggs WR., Biochemistry 39(31), 2000
PMID: 10924135
Structural basis of a phototropin light switch.
Harper SM, Neil LC, Gardner KH., Science 301(5639), 2003
PMID: 12970567
Disruption of the LOV-Jalpha helix interaction activates phototropin kinase activity.
Harper SM, Christie JM, Gardner KH., Biochemistry 43(51), 2004
PMID: 15610012
Structural basis for light-dependent signaling in the dimeric LOV domain of the photosensor YtvA.
Moglich A, Moffat K., J. Mol. Biol. 373(1), 2007
PMID: 17764689
Structural basis of photosensitivity in a bacterial light-oxygen-voltage/helix-turn-helix (LOV-HTH) DNA-binding protein.
Nash AI, McNulty R, Shillito ME, Swartz TE, Bogomolni RA, Luecke H, Gardner KH., Proc. Natl. Acad. Sci. U.S.A. 108(23), 2011
PMID: 21606338
Structure of a light-activated LOV protein dimer that regulates transcription.
Vaidya AT, Chen CH, Dunlap JC, Loros JJ, Crane BR., Sci Signal 4(184), 2011
PMID: 21868352
AUREOCHROME, a photoreceptor required for photomorphogenesis in stramenopiles.
Takahashi F, Yamagata D, Ishikawa M, Fukamatsu Y, Ogura Y, Kasahara M, Kiyosue T, Kikuyama M, Wada M, Kataoka H., Proc. Natl. Acad. Sci. U.S.A. 104(49), 2007
PMID: 18003911
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
Structure of a Native-like Aureochrome 1a LOV Domain Dimer from Phaeodactylum tricornutum.
Banerjee A, Herman E, Kottke T, Essen LO., Structure 24(1), 2015
PMID: 26688213
AUREOCHROME1a-mediated induction of the diatom-specific cyclin dsCYC2 controls the onset of cell division in diatoms (Phaeodactylum tricornutum).
Huysman MJ, Fortunato AE, Matthijs M, Costa BS, Vanderhaeghen R, Van den Daele H, Sachse M, Inze D, Bowler C, Kroth PG, Wilhelm C, Falciatore A, Vyverman W, De Veylder L., Plant Cell 25(1), 2013
PMID: 23292736
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
Spatio-temporally precise activation of engineered receptor tyrosine kinases by light.
Grusch M, Schelch K, Riedler R, Reichhart E, Differ C, Berger W, Ingles-Prieto A, Janovjak H., EMBO J. 33(15), 2014
PMID: 24986882
Light-assisted small-molecule screening against protein kinases.
Ingles-Prieto A, Reichhart E, Muellner MK, Nowak M, Nijman SM, Grusch M, Janovjak H., Nat. Chem. Biol. 11(12), 2015
PMID: 26457372
Crystal structures of Aureochrome1 LOV suggest new design strategies for optogenetics.
Mitra D, Yang X, Moffat K., Structure 20(4), 2012
PMID: 22483116
Blue light-induced LOV domain dimerization enhances the affinity of Aureochrome 1a for its target DNA sequence.
Heintz U, Schlichting I., Elife 5(), 2016
PMID: 26754770
Blue-light-induced unfolding of the Jα helix allows for the dimerization of aureochrome-LOV from the diatom Phaeodactylum tricornutum.
Herman E, Sachse M, Kroth PG, Kottke T., Biochemistry 52(18), 2013
PMID: 23621750
Allosterically regulated unfolding of the A'α helix exposes the dimerization site of the blue-light-sensing aureochrome-LOV domain.
Herman E, Kottke T., Biochemistry 54(7), 2015
PMID: 25621532
Photoreactions of aureochrome-1.
Toyooka T, Hisatomi O, Takahashi F, Kataoka H, Terazima M., Biophys. J. 100(11), 2011
PMID: 21641326
A novel type of light-harvesting antenna protein of red algal origin in algae with secondary plastids.
Sturm S, Engelken J, Gruber A, Vugrinec S, Kroth PG, Adamska I, Lavaud J., BMC Evol. Biol. 13(), 2013
PMID: 23899289
Identification and evaluation of endogenous reference genes for steady state transcript quantification by qPCR in the diatom Phaeodactlyum tricornutum with constitutive expression independent from time and ligh
Sachse, J. Endocytobiosis Cell Res. 24(), 2013
Upgraded ESRF BM29 beamline for SAXS on macromolecules in solution.
Pernot P, Round A, Barrett R, De Maria Antolinos A, Gobbo A, Gordon E, Huet J, Kieffer J, Lentini M, Mattenet M, Morawe C, Mueller-Dieckmann C, Ohlsson S, Schmid W, Surr J, Theveneau P, Zerrad L, McSweeney S., J Synchrotron Radiat 20(Pt 4), 2013
PMID: 23765312
New developments in the ATSAS program package for small-angle scattering data analysis
Petoukhov MV, Franke D, Shkumatov AV, Tria G, Kikhney AG, Gajda M, Gorba C, Mertens HDT, Konarev PV, Svergun DI., J Appl Crystallogr 45(), 2012
PMID: c7010
Development and testing of a general amber force field.
Wang J, Wolf RM, Caldwell JW, Kollman PA, Case DA., J Comput Chem 25(9), 2004
PMID: 15116359
Taking into Account the Ion-induced Dipole Interaction in the Nonbonded Model of Ions.
Li P, Merz KM Jr., J Chem Theory Comput 10(1), 2014
PMID: 24659926
A core-weighted fitting method for docking atomic structures into low-resolution maps: application to cryo-electron microscopy.
Wu X, Milne JL, Borgnia MJ, Rostapshov AV, Subramaniam S, Brooks BR., J. Struct. Biol. 141(1), 2003
PMID: 12576021
Targeted conformational search with map-restrained self-guided Langevin dynamics: application to flexible fitting into electron microscopic density maps.
Wu X, Subramaniam S, Case DA, Wu KW, Brooks BR., J. Struct. Biol. 183(3), 2013
PMID: 23876978
Structural specificity in coiled-coil interactions.
Grigoryan G, Keating AE., Curr. Opin. Struct. Biol. 18(4), 2008
PMID: 18555680
What vibrations tell us about proteins.
Barth A, Zscherp C., Q. Rev. Biophys. 35(4), 2002
PMID: 12621861
Conformational heterogeneity and propagation of structural changes in the LOV2/Jalpha domain from Avena sativa phototropin 1 as recorded by temperature-dependent FTIR spectroscopy.
Alexandre MT, van Grondelle R, Hellingwerf KJ, Kennis JT., Biophys. J. 97(1), 2009
PMID: 19580761
Light signal transduction pathway from flavin chromophore to the J alpha helix of Arabidopsis phototropin1.
Yamamoto A, Iwata T, Sato Y, Matsuoka D, Tokutomi S, Kandori H., Biophys. J. 96(7), 2009
PMID: 19348760
Blue light induces global and localized conformational changes in the kinase domain of full-length phototropin.
Pfeifer A, Mathes T, Lu Y, Hegemann P, Kottke T., Biochemistry 49(5), 2010
PMID: 20052995
Consensus and variant cAMP-regulated enhancers have distinct CREB-binding properties.
Craig JC, Schumacher MA, Mansoor SE, Farrens DL, Brennan RG, Goodman RH., J. Biol. Chem. 276(15), 2000
PMID: 11134034
Magnesium is required for specific DNA binding of the CREB B-ZIP domain.
Moll JR, Acharya A, Gal J, Mir AA, Vinson C, Gal J., Nucleic Acids Res. 30(5), 2002
PMID: 11861917
Enhanced DNA-binding activity of a Stat3-related protein in cells transformed by the Src oncoprotein.
Yu CL, Meyer DJ, Campbell GS, Larner AC, Carter-Su C, Schwartz J, Jove R., Science 269(5220), 1995
PMID: 7541555
Plant bZIP proteins gather at ACGT elements.
Foster R, Izawa T, Chua NH., FASEB J. 8(2), 1994
PMID: 8119490
Mutation of either G box or I box sequences profoundly affects expression from the Arabidopsis rbcS-1A promoter.
Donald RG, Cashmore AR., EMBO J. 9(6), 1990
PMID: 2347304
Abscisic acid-responsive sequences from the em gene of wheat.
Marcotte WR Jr, Russell SH, Quatrano RS., Plant Cell 1(10), 1989
PMID: 2562556
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
The GCN4 bZIP can bind to noncognate gene regulatory sequences.
Fedorova AV, Chan IS, Shin JA., Biochim. Biophys. Acta 1764(7), 2006
PMID: 16784907
Determination of the secondary structure content of proteins in aqueous solutions from their amide I and amide II infrared bands. Comparison between classical and partial least-squares methods.
Dousseau F, Pezolet M., Biochemistry 29(37), 1990
PMID: 2271555
FTIR-Spectroscopy of multistranded coiled coil proteins.
Heimburg T, Schunemann J, Weber K, Geisler N., Biochemistry 38(39), 1999
PMID: 10504243
Crystal structure of a bZIP/DNA complex at 2.2 A: determinants of DNA specific recognition.
Keller W, Konig P, Richmond TJ., J. Mol. Biol. 254(4), 1995
PMID: 7500340
CRYSOL - A program to evaluate x-ray solution scattering of biological macromolecules from atomic coordinates
Svergun D, Barberato C, Koch MHJ., J Appl Crystallogr 28(), 1995
PMID: c7007
The GCN4 basic region leucine zipper binds DNA as a dimer of uninterrupted alpha helices: crystal structure of the protein-DNA complex.
Ellenberger TE, Brandl CJ, Struhl K, Harrison SC., Cell 71(7), 1992
PMID: 1473154
The structure of a CREB bZIP.somatostatin CRE complex reveals the basis for selective dimerization and divalent cation-enhanced DNA binding.
Schumacher MA, Goodman RH, Brennan RG., J. Biol. Chem. 275(45), 2000
PMID: 10952992
Simulations of temperature and salt concentration effects on bZIP, a basic region leucine zipper.
Cukier RI., J Phys Chem B 116(21), 2012
PMID: 22559083
Bending and adaptability to proteins of the cAMP DNA-responsive element: molecular dynamics contrasted with NMR.
Derreumaux S, Fermandjian S., Biophys. J. 79(2), 2000
PMID: 10920000
DNA looping induced by a transcriptional enhancer in vivo.
Petrascheck M, Escher D, Mahmoudi T, Verrijzer CP, Schaffner W, Barberis A., Nucleic Acids Res. 33(12), 2005
PMID: 16002789
DNA looping between sites for transcriptional activation: self-association of DNA-bound Sp1.
Su W, Jackson S, Tjian R, Echols H., Genes Dev. 5(5), 1991
PMID: 1851121
The acclimation of Phaeodactylum tricornutum to blue and red light does not influence the photosynthetic light reaction but strongly disturbs the carbon allocation pattern.
Jungandreas A, Schellenberger Costa B, Jakob T, von Bergen M, Baumann S, Wilhelm C., PLoS ONE 9(8), 2014
PMID: 25111046
Relative expression software tool (REST) for group-wise comparison and statistical analysis of relative expression results in real-time PCR.
Pfaffl MW, Horgan GW, Dempfle L., Nucleic Acids Res. 30(9), 2002
PMID: 11972351
Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®
Quellen

PMID: 27179025
PubMed | Europe PMC

Suchen in

Google Scholar