Bacillus licheniformis Contains Two More PerR-Like Proteins in Addition to PerR, Fur, and Zur Orthologues

Abstract

The ferric uptake regulator (Fur) family proteins include sensors of Fe (Fur), Zn (Zur), and peroxide (PerR). Among Fur family proteins, Fur and Zur are ubiquitous in most prokaryotic organisms, whereas PerR exists mainly in Gram positive bacteria as a functional homologue of OxyR. Gram positive bacteria such as Bacillus subtilis, Listeria monocytogenes and Staphylococcus aureus encode three Fur family proteins: Fur, Zur, and PerR. In this study, we identified five Fur family proteins from B. licheniformis: two novel PerR-like proteins (BL00690 and BL00950) in addition to Fur (BL05249), Zur (BL03703), and PerR (BL00075) homologues. Our data indicate that all of the five B. licheniformis Fur homologues contain a structural Zn2+ site composed of four cysteine residues like many other Fur family proteins. Furthermore, we provide evidence that the PerR-like proteins (BL00690 and BL00950) as well as PerRBL (BL00075), but not FurBL (BL05249) and ZurBL (BL03703), can sense H2O2 by histidine oxidation with different sensitivity. We also show that PerR2 (BL00690) has a PerR-like repressor activity for PerR-regulated genes in vivo. Taken together, our results suggest that B. licheniformis contains three PerR subfamily proteins which can sense H2O2 by histidine oxidation not by cysteine oxidation, in addition to Fur and Zur.

Roles of three FurA paralogs in the regulation of genes pertaining to peroxide defense in Mycobacterium smegmatis mc2155

“…S2–S7). The level of His oxidation observed for the three FurA paralogs was comparable to that of PerR proteins treated by H 2 O 2 under the same experimental conditions (Won et al ., ; Kim et al ., ). The high sensitivity of the three FurA paralogs to His oxidation by H 2 O 2 suggests that they are rapidly inactivated by H 2 O 2 through MCHO like PerR proteins.…”

“…The oxidation status of FurA proteins was analyzed by MALDI‐TOF MS and LC‐ESI MS/MS. As described previously (Kim et al ., ), aliquots of E. coli BL21 (DE3) cells (1.8 ml of cultures of the strains harboring pET29bfurA1, pET29bfurA2 or pET29bfurA3) were treated with either 100 μM H 2 O 2 (final concentration) or the same volume of distilled water for 1 min. Cells were harvested by centrifugation after the addition of 200 μl of 100% (wt/vol) trichloroacetic acid (TCA) solution.…”

The oxidative stress response of pathogenic Leptospira is controlled by two peroxide stress regulators which putatively cooperate in controlling virulence

“…The coexistence of three PerR-like regulators has been reported only in Gram-positive bacteria such as B. licheniformis and M. smegmatis . It was shown that the three B. licheniformis PerRs sense hydrogen peroxide by histidine oxidation, although with different sensitivity [55]. In M. smegmatis , three Fur-like paralogs displayed the canonical PerR Asp residue involved in H 2 O 2 sensitivity, exhibited H 2 O 2 sensing by metal-catalyzed histidine oxidation and a higher H 2 O 2 resistance when their genes were inactivated [56].…”

Comparative Genomics of Bacillus amyloliquefaciens Strains Reveals a Core Genome with Traits for Habitat Adaptation and a Secondary Metabolites Rich Accessory Genome

“…The nitrogenase-encoding genes nifHDK, nifS , and nifU responsible for nitrogen fixation in proteobacterial PGPR from Azospirillum, Burkholderia , and Bacillus were used as bait to search for similar sequences (Bruto et al, 2014 ). The pyrroloquinoline quinone-encoding genes pqqBCDEFG in the PGPR Pseudomonas fluorescens F113, Erwinia herbicola , and Enterobacter intermedium (Liu et al, 1992 and Kim et al, 2003 ; Miller et al, 2010 ) were used to mine the studied genomes. The gene encoding the B. velezensis SQR9 3-phytase was selected to mine B. amyloliquefaciens genomes for phytase production (Shao et al, 2015 ).…”