2008
DOI: 10.1002/cbic.200800280
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Influence of a Joining Helix on the BLUF Domain of the YcgF Photoreceptor from Escherichia coli

Abstract: BLUF-domain-comprising photoreceptors sense blue light by utilizing FAD as a chromophore. The ycgF gene product of Escherichia coli is composed of a N-terminal BLUF domain and a C-terminal EAL domain, with the latter postulated to catalyze c-di-GMP hydrolysis. The linkage between these two domains involves a predominantly helical segment. Its role on the function of the YcgF photoreceptor domain was examined by characterizing BLUF domains with and without this segment and reconstituting them with either FAD, F… Show more

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Cited by 26 publications
(36 citation statements)
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“…These data suggest high affinities and low off-rates of the interaction reactions involved. This is also consistent with no rebinding of YcgE to ycgZ p DNA, when samples treated as in Figure 3A were kept in the dark for 60 min before running them on the gel (data not shown), and the slow reversion to the ground state in the photocycle of YcgF (Schroeder et al 2008). In the absence of blue-light irradiation, even a relatively large excess of YcgF did not release YcgE from its operator.…”
Section: Identification Of Target Genes Of the Merr-like Regulator Ycgesupporting
confidence: 75%
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“…These data suggest high affinities and low off-rates of the interaction reactions involved. This is also consistent with no rebinding of YcgE to ycgZ p DNA, when samples treated as in Figure 3A were kept in the dark for 60 min before running them on the gel (data not shown), and the slow reversion to the ground state in the photocycle of YcgF (Schroeder et al 2008). In the absence of blue-light irradiation, even a relatively large excess of YcgF did not release YcgE from its operator.…”
Section: Identification Of Target Genes Of the Merr-like Regulator Ycgesupporting
confidence: 75%
“…We noted that low temperature induction of ycgF expression is clearly stronger than that of ycgE (;30-fold and sevenfold, respectively, when cells were shifted from 37°C to 16°C). Blue light promotes a conformational change of YcgF (Hasegawa et al 2006;Nakasone et al 2007;Schroeder et al 2008) that probably increases YcgF affinity for YcgE and allows it to release YcgE from its operator site (as discussed above). Yet, by simple mass action, the cold-induced increase in the YcgF:YcgE stoichiometry also could have similar consequences; i.e., generate enough active YcgF to sequester YcgE and therefore induce the YcgE regulon.…”
Section: Discussionmentioning
confidence: 99%
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“…A direct inhibitory effect of the uncomplexed PAS-like domain appears unlikely, because it is rather remote from the ␤5-␣5 loop. For the same reason, direct transmission of the information by the domain linking helix seems unlikely, although light-induced structural changes in the joining helix have been seen for a fragment of the BLUF-EAL protein YcgF by NMR (52). However, impact of the state of the PAS domain on the quaternary arrangement of YkuI (possibly transmitted by the linking helix) appears possible.…”
Section: C-di-gmp-specific Phosphodiesterasementioning
confidence: 99%