AhpA is a peroxidase expressed during biofilm formation in Bacillus subtilis
| Autor: | Sarah Noble, Yasser K. Ellaicy, Dylan J. Hakey, Alyssa N. King, Gabrielle Dierker Coe, Joelie V. Zwick, Alex J. Sadauskas, Melinda J. Faulkner |
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| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
sporulation 030106 microbiology Mutant Bacillus subtilis peroxide Microbiology Spo0A 03 medical and health sciences AhpC Bacterial Proteins Derepression Original Research chemistry.chemical_classification Spores Bacterial Reactive oxygen species biology Biofilm peroxiredoxin Hydrogen Peroxide AbrB biology.organism_classification DNA-Binding Proteins Oxidative Stress 030104 developmental biology Enzyme Biochemistry chemistry Peroxidases Biofilms biology.protein biofilm formation Peroxiredoxin alkylhydroperoxide reductase Peroxidase DNA Damage Transcription Factors |
| Zdroj: | MicrobiologyOpen |
| ISSN: | 2045-8827 |
| Popis: | Organisms growing aerobically generate reactive oxygen species such as hydrogen peroxide. These reactive oxygen molecules damage enzymes and DNA, potentially causing cell death. In response, Bacillus subtilis produces at least nine potential peroxide‐scavenging enzymes; two belong to the alkylhydroperoxide reductase (Ahp) class of peroxidases. Here, we explore the role of one of these Ahp homologs, AhpA. While previous studies demonstrated that AhpA can scavenge peroxides and thus defend cells against peroxides, they did not clarify when during growth the cell produces AhpA. The results presented here show that the expression of ahpA is regulated in a manner distinct from that of the other peroxide‐scavenging enzymes in B. subtilis. While the primary Ahp, AhpC, is expressed during exponential growth and stationary phase, these studies demonstrate that the expression of ahpA is dependent on the transition‐state regulator AbrB and the sporulation and biofilm formation transcription factor Spo0A. Furthermore, these results show that ahpA is specifically expressed during biofilm formation, and not during sporulation or stationary phase, suggesting that derepression of ahpA by AbrB requires a signal other than those present upon entry into stationary phase. Despite this expression pattern, ahpA mutant strains still form and maintain robust biofilms, even in the presence of peroxides. Thus, the role of AhpA with regard to protecting cells within biofilms from environmental stresses is still uncertain. These studies highlight the need to further study the Ahp homologs to better understand how they differ from one another and the unique roles they may play in oxidative stress resistance. |
| Databáze: | OpenAIRE |
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