Schematic drawing of the CelR regulator and proposed model for regulation.

<p>Panel (A) shows the CelR regulator composed of a helix-turn-helix (HTH) domain, a M trans-acting positive regulator (Mga) domain, two PTS-regulatory domain (PRD), and phosphotransferase system EIIB<sup>Gat-like</sup> and EIIA<sup>Mtl</sup> domains <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047393#pone.0047393-Finn1" target="_blank">[26]</a>. The phosphorylable conserved residues, five histidine and one cysteine, are shown <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047393#pone.0047393-Zeng1" target="_blank">[8]</a>, <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047393#pone.0047393-Joyet1" target="_blank">[17]</a>. Panel (B) shows the proposed regulatory circuit in presence of cellobiose and absence of glucose. In such a situation in <i>S. mutans</i> HPr protein does not phosphorylate the glucose transporter (pneumococcal orthologue spr0259-60-61), but phosphorylates the cellobiose PTS (pneumococcal orthologue spr0278-80-82) and the CelR regulator <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047393#pone.0047393-Zeng1" target="_blank">[8]</a>. In addition the cellobiose PTS does also dephosphorylate CelR <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047393#pone.0047393-Zeng1" target="_blank">[8]</a>. Phosphorylation in presence of cellobiose of the second beta-glucoside PTS <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0047393#pone.0047393-Bidossi1" target="_blank">[5]</a> is in accordance with gene expression data (Safeeq and Kuipers, personal communication). Phosphorylation of the CelR EIIB domain phosphorylable cysteine by the CelR EIIA domain is deduced from our growth phenotypes. The putative interaction of the spr0505 EIIBA domains with the PRD domains of CelR is shown as dashed line.</p>

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