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Oxygen-regulated expression of genes for pigment binding proteins in Rhodobacter capsulatus.J. Mol. Light-dependent repression of photosynthesis genes in R. sphaeroides beneath semiaerobic circumstances depends on the presence of the PrrA response regulator. Recently, we revealed that signal transmission by AppA requires a heme cofactor (Y. Han, M. Meyer, M. Keusgen, and G. Klug, submitted for publication). The ranges of proteins with sure heme may be elevated if E.
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The expression values at low oxygen have been divided by the expression levels of a control saved at high oxygen rigidity, and the relative change in this value compared to time level zero was plotted. Response of puc expression to blue-mild illumination of Paracoccus denitrificans expressing the appA and ppsR genes or the ppsR gene solely . Light illumination started at time level zero, and expression of a puc-lux reporter gene was adopted by determination of luminescence. Expression values within the light have been divided by expression ranges of a management saved at midnight, and the relative change on this value in comparison with time level zero was plotted. Results for a single representative experiment are given.
coli-type promoters. Therefore, expression of AppA and PpsR in other bacteria does not establish blue-light signaling. It seems that the presence of AppA interferes with PpsR repression even at excessive oxygen tension in E. coli, and no redox-dependent change in AppA-PpsR interaction occurs. Based on earlier reviews, it is unlikely that the cytoplasmic redox potential of Rhodobacter is less lowered than that of E. We demonstrated recently that a heme cofactor hooked up to AppA is concerned in redox and lightweight signaling (Han et al., submitted).