suis serotype 2 strain 05ZYH33 (GenBank accession no. CP000407). This PLX4032 datasheet protein has been defined as a zinc uptake regulator (Zur) [18], as well as an iron uptake regulator (Fur) in S. suis[19], but the research

on its function in oxidative stress response is limited, whereas its homolog in Streptococcus pyogenes has been demonstrated to be a peroxide regulon repressor PerR [20–22]. In this study, the role of this Fur-like protein in peroxide resistance was confirmed in S. suis serotype 2. Therefore, we renamed this protein as PerR. At the same time, two target operons, dpr (dps-like peroxide resistance protein) and metNIQ (methionine ABC-type transporter), were identified and proved to play important roles in oxidative stress response. Results Identification of a fur-like protein in S. Suis and other streptococci In the genome of 05ZYH33 (a strain of S. suis serotype 2), the Fur-like protein encoded by SSU05_0310 had been

first identified as Tozasertib a Zur [18], and we found that SSU05_0310 is the sole EPZ015938 gene encoding a Fur-like protein in S. suis 05ZYH33. The SSU05_0310 protein consisted of 151 amino acids and contained a DNA-binding motif (Figure 1A). To identify the Fur-like proteins in other streptococci, a BLAST homology search using the sequence of SSU05_0310 was performed among the sequenced genomes of the members of genus Streptococcus. All streptococci had a single conserved Fur-like protein except that no Fur-like protein was found in Streptococcus pneumoniae. All the Fur-like proteins in streptococci and their homologs (Fur, Zur and PerR) in B. subtilis S. aureus and C. acetobutylicum were used for cluster analysis, the result medroxyprogesterone showed that the Fur-like proteins in streptococci

clustered in the PerR group (Figure 1B). Furthermore, through sequence analysis, the key amino acid residues of PerR for H2O2 response and metal ions binding were highly conserved in SSU05_0310 protein (Figure 1A) [23]. Consequently, we named the single Fur-like protein in S. suis as PerR. Figure 1 Fur-like proteins are conserved among the genus Streptococcus and are close to PerR. (A) Multiple alignment of PerR protein from S. suis 05ZYH33 with the Fur family proteins PerR, Zur and Fur in B. subtilis str. 168. The DNA-binding motif is marked in the gray box. Nine conserved amino acid residues in PerR are marked with gray bottom colour. Five residues (H37, D85, H91, H93 and D104) are the candidate amino acid ligands for Fe2+ or Mn2+ and four cysteine residues (C96, C99, C136 and C139) are for Zn2+, H37 and H91 are the sites of H2O2-mediated oxidation. These amino acid residues in S. suis PerR protein are conserved except that N is taking the place of H in site 93, this change also exists in S. pyogenes. (B) A phylogenetic tree of Fur-like proteins from selected streptococci and other Gram-positive bacteria was constructed based on a multiple sequence alignment using DNAMAN.