PhoU homologs from Staphylococcus aureus dimerization and protein interactions
ABSTRACT PhoU proteins are negative regulators of the phosphate response, regulate virulence, and contribute to antibiotic resistance. Staphylococcus aureus has multiple genes encoding PhoU homologs that regulate persister formation and potentially virulence, but the molecular mechanisms of this reg...
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American Society for Microbiology
2025-01-01
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| Series: | Microbiology Spectrum |
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| Online Access: | https://journals.asm.org/doi/10.1128/spectrum.02067-24 |
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| author | Clayton T. Matthews Sakib Mahmud Stewart G. Gardner |
| author_facet | Clayton T. Matthews Sakib Mahmud Stewart G. Gardner |
| author_sort | Clayton T. Matthews |
| collection | DOAJ |
| description | ABSTRACT PhoU proteins are negative regulators of the phosphate response, regulate virulence, and contribute to antibiotic resistance. Staphylococcus aureus has multiple genes encoding PhoU homologs that regulate persister formation and potentially virulence, but the molecular mechanisms of this regulation are not fully understood. We used a bacterial adenylate cyclase two-hybrid system to assess interactions between PhoU homologs and other proteins known to interact with PhoU from Escherichia coli. S. aureus PhoU (also referred to as PhoU1) interacted with PhoU itself; PitR (also referred to as PhoU2) interacted with PitR itself. We identified potential structural and dimerization models for S. aureus PhoU homologs. Dimerization was confirmed using size exclusion chromatography of purified proteins. These results highlight the complex nature of PhoU proteins. Further analysis may elucidate the potential mechanisms for regulating gene expression, persister formation, and virulence in S. aureus.IMPORTANCEPhoU proteins affect pathogenesis and persister formation in many bacterial species. This protein is essential for signaling environmental phosphate levels in Escherichia coli but is still not well characterized in many other pathogenic bacterial strains. This work identifies some similarities and key differences in Staphylococcus aureus PhoU homologs compared to E. coli PhoU, specifically, PhoU and PitR from S. aureus form homodimers but do not appear to interact with PhoR or phosphate transporter proteins. |
| format | Article |
| id | doaj-art-600383bf9da24cd5b165d797eec443fc |
| institution | Kabale University |
| issn | 2165-0497 |
| language | English |
| publishDate | 2025-01-01 |
| publisher | American Society for Microbiology |
| record_format | Article |
| series | Microbiology Spectrum |
| spelling | doaj-art-600383bf9da24cd5b165d797eec443fc2025-01-07T14:05:19ZengAmerican Society for MicrobiologyMicrobiology Spectrum2165-04972025-01-0113110.1128/spectrum.02067-24PhoU homologs from Staphylococcus aureus dimerization and protein interactionsClayton T. Matthews0Sakib Mahmud1Stewart G. Gardner2School of Science + Mathematics, Emporia State University, Emporia, Kansas, USASchool of Science + Mathematics, Emporia State University, Emporia, Kansas, USASchool of Science + Mathematics, Emporia State University, Emporia, Kansas, USAABSTRACT PhoU proteins are negative regulators of the phosphate response, regulate virulence, and contribute to antibiotic resistance. Staphylococcus aureus has multiple genes encoding PhoU homologs that regulate persister formation and potentially virulence, but the molecular mechanisms of this regulation are not fully understood. We used a bacterial adenylate cyclase two-hybrid system to assess interactions between PhoU homologs and other proteins known to interact with PhoU from Escherichia coli. S. aureus PhoU (also referred to as PhoU1) interacted with PhoU itself; PitR (also referred to as PhoU2) interacted with PitR itself. We identified potential structural and dimerization models for S. aureus PhoU homologs. Dimerization was confirmed using size exclusion chromatography of purified proteins. These results highlight the complex nature of PhoU proteins. Further analysis may elucidate the potential mechanisms for regulating gene expression, persister formation, and virulence in S. aureus.IMPORTANCEPhoU proteins affect pathogenesis and persister formation in many bacterial species. This protein is essential for signaling environmental phosphate levels in Escherichia coli but is still not well characterized in many other pathogenic bacterial strains. This work identifies some similarities and key differences in Staphylococcus aureus PhoU homologs compared to E. coli PhoU, specifically, PhoU and PitR from S. aureus form homodimers but do not appear to interact with PhoR or phosphate transporter proteins.https://journals.asm.org/doi/10.1128/spectrum.02067-24PhoU1PhoU2PitRStaphylococcus aureusBACTHdimerization |
| spellingShingle | Clayton T. Matthews Sakib Mahmud Stewart G. Gardner PhoU homologs from Staphylococcus aureus dimerization and protein interactions Microbiology Spectrum PhoU1 PhoU2 PitR Staphylococcus aureus BACTH dimerization |
| title | PhoU homologs from Staphylococcus aureus dimerization and protein interactions |
| title_full | PhoU homologs from Staphylococcus aureus dimerization and protein interactions |
| title_fullStr | PhoU homologs from Staphylococcus aureus dimerization and protein interactions |
| title_full_unstemmed | PhoU homologs from Staphylococcus aureus dimerization and protein interactions |
| title_short | PhoU homologs from Staphylococcus aureus dimerization and protein interactions |
| title_sort | phou homologs from staphylococcus aureus dimerization and protein interactions |
| topic | PhoU1 PhoU2 PitR Staphylococcus aureus BACTH dimerization |
| url | https://journals.asm.org/doi/10.1128/spectrum.02067-24 |
| work_keys_str_mv | AT claytontmatthews phouhomologsfromstaphylococcusaureusdimerizationandproteininteractions AT sakibmahmud phouhomologsfromstaphylococcusaureusdimerizationandproteininteractions AT stewartggardner phouhomologsfromstaphylococcusaureusdimerizationandproteininteractions |