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The Switch that Does Not Flip: The Blue-Light Receptor YtvA from Bacillus subtilis Adopts an Elongated Dimer Conformation Independent of the Activation State as Revealed by a Combined AUC and SAXS Study
被引:31
作者:
Jurk, Marcel
[1
,2
]
Dorn, Matthias
[1
]
Kikhney, Alexey
[3
]
Svergun, Dmitri
[3
]
Gaertner, Wolfgang
[4
]
Schmieder, Peter
[1
]
机构:
[1] Leibniz Inst Mol Pharmacol, D-13125 Berlin, Germany
[2] Free Univ Berlin, Inst Chem & Biochem, D-14195 Berlin, Germany
[3] European Mol Biol Lab, D-22603 Hamburg, Germany
[4] Max Planck Inst Bioanorgan Chem, D-45470 Mulheim, Germany
关键词:
YtvA;
photoreceptor;
SAXS;
AUC;
oligomerization state;
SMALL-ANGLE SCATTERING;
GENERAL STRESS-RESPONSE;
STRUCTURAL BASIS;
LOV DOMAIN;
BIOLOGICAL MACROMOLECULES;
ARABIDOPSIS PHOTOTROPIN-1;
TRANSCRIPTION FACTOR;
PROTEIN;
CHROMOPHORE;
PHOTORECEPTOR;
D O I:
10.1016/j.jmb.2010.08.036
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Photoreceptors play an important role in plants and bacteria by converting extracellular stimuli into intracellular signals. One distinct class are the blue-light-sensitive phototropins harboring a light oxygen voltage (LOV) domain coupled to various effector domains. Photon absorption by the chromophore within the LOV domain results in an activation of the output domain via mechanisms that are hitherto not well understood. The photoreceptor YtvA from Bacillus subtilis is a bacterial analog of phototropins, consists of an LOV and a sulfate transporter/anti-sigma factor antagonist domain, and is involved in the response of the bacterium to environmental stress. We present here analytical ultracentrifugation studies and small-angle X-ray scattering experiments, showing that YtvA is a dimer. On the basis of these results, we present a low-resolution model of the dimer in the dark and the lit state of the protein. In addition, we show that YtvA does not change its oligomerization state or its overall shape upon light activation. (C) 2010 Elsevier Ltd. All rights reserved.
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页码:78 / 87
页数:10
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