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The sporulation inhibitor activity of NprR relies on Spo0F dephosphorylation.

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posted on 02.08.2016, 04:30 authored by Stéphane Perchat, Antoine Talagas, Sandrine Poncet, Noureddine Lazar, Inès Li de la Sierra-Gallay, Michel Gohar, Didier Lereclus, Sylvie Nessler

(A) Microscale thermophoresis analysis of the NprR-Spo0F interaction. The normalized NprR fluorescence Fnorm, i.e. the “hot” fluorescence divided by the “cold” fluorescence, is plotted on a linear y-axis in per mil (‰) against the total concentration of Spo0F on a log10 x-axis. The measurements were performed by using 20% LED power and 40% IR-laser power, in the presence (green triangles) and absence (blue squares) of NprX. (B) In vitro dephosphorylation of Spo0F-P by NprR. Purified B. subtilis Spo0F proteins (5.4 μM) was phosphorylated in a reaction containing B. subtilis KinA (0.1 μM) and [γ-32P]-ATP. Purified NprR protein and synthetic NprX-8 peptide (SSKPDIVG) were added at 10 μM and 57 μM final concentration, respectively. Time course experiments were carried out and aliquots withdrawn at the indicated time points.

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