Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains.
Horizontal transfer of mobile genetic elements within Staphylococci is of high biomedical significance as such elements are frequently responsible for virulence and toxic effects. Staphylococcus-encoded repressor proteins regulate the replication of these mobile genetic elements that are located wit...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2015-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC4634304?pdf=render |
| _version_ | 1818533712295362560 |
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| author | Kinga Nyíri Bianka Kőhegyi András Micsonai József Kardos Beata G Vertessy |
| author_facet | Kinga Nyíri Bianka Kőhegyi András Micsonai József Kardos Beata G Vertessy |
| author_sort | Kinga Nyíri |
| collection | DOAJ |
| description | Horizontal transfer of mobile genetic elements within Staphylococci is of high biomedical significance as such elements are frequently responsible for virulence and toxic effects. Staphylococcus-encoded repressor proteins regulate the replication of these mobile genetic elements that are located within the so-called pathogenicity islands. Here, we report structural and functional characterization of one such repressor protein, namely the Stl protein encoded by the pathogenicity island SaPIbov1. We create a 3D structural model and based on this prediction, we investigate the different functionalities of truncated and point mutant constructs. Results suggest that a helix-turn-helix motif governs the interaction of the Stl protein with its cognate DNA site: point mutations within this motif drastically decrease DNA-binding ability, whereas the interaction with the Stl-binding partner protein dUTPase is unperturbed by these point mutations. The 3D model also suggested the potential independent folding of a carboxy-terminal domain. This suggestion was fully verified by independent experiments revealing that the carboxy-terminal domain does not bind to DNA but is still capable of binding to and inhibiting dUTPase. A general model is proposed, which suggests that among the several structurally different repressor superfamilies Stl-like Staphylococcal repressor proteins belong to the helix-turn-helix transcription factor group and the HTH motif is suggested to reside within N-terminal segment. |
| first_indexed | 2024-12-11T18:02:21Z |
| format | Article |
| id | doaj.art-cd829d8506d84f60acccd45b8f4b916c |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T18:02:21Z |
| publishDate | 2015-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-cd829d8506d84f60acccd45b8f4b916c2022-12-22T00:55:51ZengPublic Library of Science (PLoS)PLoS ONE1932-62032015-01-01109e013908610.1371/journal.pone.0139086Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains.Kinga NyíriBianka KőhegyiAndrás MicsonaiJózsef KardosBeata G VertessyHorizontal transfer of mobile genetic elements within Staphylococci is of high biomedical significance as such elements are frequently responsible for virulence and toxic effects. Staphylococcus-encoded repressor proteins regulate the replication of these mobile genetic elements that are located within the so-called pathogenicity islands. Here, we report structural and functional characterization of one such repressor protein, namely the Stl protein encoded by the pathogenicity island SaPIbov1. We create a 3D structural model and based on this prediction, we investigate the different functionalities of truncated and point mutant constructs. Results suggest that a helix-turn-helix motif governs the interaction of the Stl protein with its cognate DNA site: point mutations within this motif drastically decrease DNA-binding ability, whereas the interaction with the Stl-binding partner protein dUTPase is unperturbed by these point mutations. The 3D model also suggested the potential independent folding of a carboxy-terminal domain. This suggestion was fully verified by independent experiments revealing that the carboxy-terminal domain does not bind to DNA but is still capable of binding to and inhibiting dUTPase. A general model is proposed, which suggests that among the several structurally different repressor superfamilies Stl-like Staphylococcal repressor proteins belong to the helix-turn-helix transcription factor group and the HTH motif is suggested to reside within N-terminal segment.http://europepmc.org/articles/PMC4634304?pdf=render |
| spellingShingle | Kinga Nyíri Bianka Kőhegyi András Micsonai József Kardos Beata G Vertessy Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains. PLoS ONE |
| title | Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains. |
| title_full | Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains. |
| title_fullStr | Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains. |
| title_full_unstemmed | Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains. |
| title_short | Evidence-Based Structural Model of the Staphylococcal Repressor Protein: Separation of Functions into Different Domains. |
| title_sort | evidence based structural model of the staphylococcal repressor protein separation of functions into different domains |
| url | http://europepmc.org/articles/PMC4634304?pdf=render |
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