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| Content Provider | Springer Nature Link |
|---|---|
| Author | Nyíri, Kinga Papp Kádár, Veronika Szabó, Judit E. Németh, Veronika Vértessy, Beáta G. |
| Copyright Year | 2015 |
| Abstract | dUTPases are essential for maintaining genome integrity. Recently, in the case of a dUTPase from a Staphylococcal phage, another different physiological function was also suggested. Namely, it was shown that dUTPase from the Staphylococcus aureus bacteriophage Ф11 is capable of binding to the Staphylococcal Stl repressor protein. This binding interferes with the function of Stl. In the present study, we investigated the putative role of a phage dUTPase-specific peptide segment in the interaction of dUTPase with Stl and in impeding Stl–DNA complex formation. We show that dUTPase from Mycobacterium tuberculosis that lacks the phage-specific insert is also capable of disrupting the complexation between Stl and DNA. Hence, the insert segment is not essential for perturbation of the Stl function. However, we also demonstrate that in case of the phage dUTPase, the insert-lacking construct is deficient in perturbation of Stl activity. These findings clearly indicate that the phage-specific insert has a well-defined role only in the context of the phage dUTPase. |
| Starting Page | 1425 |
| Ending Page | 1432 |
| Page Count | 8 |
| File Format | |
| ISSN | 10400400 |
| Journal | Structural Chemistry |
| Volume Number | 26 |
| Issue Number | 5-6 |
| e-ISSN | 15729001 |
| Language | English |
| Publisher | Springer US |
| Publisher Date | 2015-08-30 |
| Publisher Place | New York |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | dUTPase Non-canonical insert Protein–protein interaction Protein–DNA interaction Staphylococcal repressor Computer Applications in Chemistry Physical Chemistry Theoretical and Computational Chemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physical and Theoretical Chemistry Condensed Matter Physics |
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