Structural features of the single-stranded DNA-binding protein of Epstein–Barr virus
| Autor: | Jack D. Griffith, Paul A. Tucker, Dmitri I. Svergun, Eleni Mumtsidu, Alexander M. Makhov, Petr V. Konarev |
|---|---|
| Rok vydání: | 2008 |
| Předmět: |
ICP8
Protein Conformation viruses Molecular Sequence Data DNA Single-Stranded medicine.disease_cause Virus Single-stranded binding protein Viral Proteins chemistry.chemical_compound Structural Biology medicine Humans Scattering Radiation Amino Acid Sequence Sequence Deletion chemistry.chemical_classification biology X-Rays Epstein–Barr virus Molecular biology Amino acid DNA-Binding Proteins Microscopy Electron Zinc Herpes simplex virus chemistry Replication Initiation biology.protein Biophysics DNA |
| Zdroj: | Journal of Structural Biology. 161:172-187 |
| ISSN: | 1047-8477 |
| DOI: | 10.1016/j.jsb.2007.10.014 |
| Popis: | We report the structural features of a C-terminal deletion construct of the Epstein-Barr virus single-stranded DNA-binding protein, Balf2 (Balf2DeltaC), which like the herpes simplex virus I encoded protein, infected cell protein 8 (ICP8), binds non-sequence specifically to single-stranded DNA (ssDNA). ICP8, in the absence of ssDNA, assembles into long filamentous structures. Removal of the 60 C-terminal amino acids of ICP8 (ICP8DeltaC) prevents the formation of such filaments, whereas addition of circular ssDNA to ICP8DeltaC induces formation of "super helical" filaments. Balf2DeltaC, which we show is a zinc-binding protein, does not form these filaments under the same conditions but does bind ssDNA in a weakly cooperative manner. Further structural comparison of both proteins in solution by small-angle X-ray scattering shows proteins with similar molecular envelopes. One major difference is the tendency of Balf2DeltaC to dimerize on different surfaces to that used for oligomerization when binding to ssDNA, and this may have implications for the mechanism of replication initiation. |
| Databáze: | OpenAIRE |
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