The CXXC Motifs Are Essential for the Function of BosR in Borrelia burgdorferi

Discussion Structure-function analyses of numerous Fur proteins have revealed that Fur binds its target DNA as a dimer. Protein dimerization requires Zn, which is coordinated via the structural S1 site in the dimerization domain of Fur proteins. To date, it has been clearly demonstrated that different geometry and amino acid residues are used by Fur protein for coordinating Zn in the S1 site (Pohl et al., 2003; Lee and Helmann, 2006; Pecqueur et al., 2006; Traoré et al., 2006, 2009; Lucarelli et al., 2007; Ahmad et al., 2009; An et al., 2009; Carpenter et al., 2009; Jacquamet et al., 2009; Sheikh and Taylor, 2009; Davies et al., 2011; Dian et al., 2011; Shin et al., 2011; Butcher et al., 2012; Makthal et al., 2013; Troxell and Hassan, 2013; Fillat, 2014; Gilston et al., 2014; Lin et al., 2014; Deng et al., 2015). For instance, for E. coli Fur protein, the first member of the Fur family characterized, its S1 site consists of two cysteines (i.e., C92, C95) in the dimerization domain (Fillat, 2014; Seo et al., 2014). Moreover, in BsPerR, four cysteines (i.e., C96, C99, C136, and C139) in the dimerization domain form two CXXC motifs and constitute a tetrahedral Zn(Cys)4 structural site (Lee and Helmann, 2006; Traoré et al., 2006, 2009; Jacquamet et al., 2009). Previous analyses have indicated that BosR binds Zn and protein binds its DNA targets as a dimer (Boylan et al., 2003; Katona et al., 2004; Seshu et al., 2004; Samuels and Radolf, 2009; Ouyang et al., 2011,...
Source: Frontiers in cellular and infection microbiology - Category: Microbiology Source Type: research