Structure determination and domain interaction
of the photochromic protein YtvA from Bacilus subtilis
Light is an important
stimulus for plants and various bacteria. These organisms have therefore
developed a number of photoreceptors, usually consisting of a protein and an
organic cofactor, to sense light of different wavelengths. The detailed
mechanism of light perception, i.e., the "primary event" and the consecutively
following conformational changes of the receptor, are still only poorly
understood. In this project the structure and domain interaction of the
flavin-binding, blue-light photoceptor YtvA from Bacillus subtilis, that is
part of the stressosomal complex will be studied. This photoreceptor is a
two-domain protein, consisting of a LOV (light, oxygen, voltage) domain
(harboring a flavin chromophore) and a STAS (Sulphate Transporters
AntiSigma-factor antagonist) domain. Utilizing modern NMR-techniques in
conjunction with isotope-labeling, we have determined the three-dimensional
structure of YtvA, studied a variety of biophysical properties of the protein
and its domains and have attempted to propose a mechanism for the signal
transduction within the stressosome.
| M. Jurk; P.
Schramm; P. Schmieder*; "The blue-light receptor YtvA from Bacillus
subtilis is permanently incorporated into the stressosome independent of the
illumination state"; Biochem. Biophys. Res. Commun. 00, 000-000
| M. Dorn; M.
Jurk; P. Schmieder*; "Blue News Update: BODIPY-GTP Binds to the
Blue-Light Receptor YtvA While GTP Does Not"; PLoS ONE 7, e29201
| M. Jurk; M.
Dorn; P. Schmieder*; "Blue Flickers of Hope: Secondary Structure,
Dynamics and Putative Dimerisation Interface of the Blue-Light Receptor YtvA
from Bacillus subtilis"; Biochemistry 50, 8163-8171 (2011)
| M. Jurk; M.
Dorn; A. Kikhney; D. Svergun; W. Gärtner; P. Schmieder*; "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"; J. Mol. Biol. 403,
01.03.2013, Peter Schmieder