DNA-Interacting Characteristics of the Archaeal Rudiviral Protein SIRV2_Gp1
| Autor: | Clare Rollie, Eveline Peeters, M. Boon, Tessa E. F. Quax, Malcolm F. White, Rob Lavigne, Marleen Voet, David Prangishvili, Ronnie Willaert |
|---|---|
| Přispěvatelé: | Molecular Microbiology, BBSRC, University of St Andrews. School of Biology, University of St Andrews. Biomedical Sciences Research Complex, Department of Bio-engineering Sciences, Structural Biology Brussels, Microbiology, Faculty of Sciences and Bioengineering Sciences |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
QH301 Biology lcsh:QR1-502 Rudiviridae Rudiviridae/genetics Genome SIRV2 lcsh:Microbiology chemistry.chemical_compound Sulfolobus/virology Virus Release helix-turn-helix domain Helix-turn-helix doman Host cell surface biology Viral Proteins/chemistry Archaeal Viruses Sulfolobus Cell biology DNA-Binding Proteins Infectious Diseases QR355 Virology DNA-Binding Proteins/chemistry Archaeal virus archaea Protein domain NDAS Genome Viral Solfolobus Article Microbiology QH301 03 medical and health sciences Viral Proteins Protein Domains Virology DNA binding DNA/chemistry Gene QR355 Virion DNA archaeal virus biology.organism_classification Archaea 030104 developmental biology chemistry Nucleic Acid Conformation |
| Zdroj: | Viruses, Vol 9, Iss 7, p 190 (2017) Viruses Viruses, 9(7):190. MDPI AG Viruses; Volume 9; Issue 7; Pages: 190 |
| ISSN: | 1999-4915 |
| Popis: | Whereas the infection cycles of many bacterial and eukaryotic viruses have been characterized in detail, those of archaeal viruses remain largely unexplored. Recently, studies on a few model archaeal viruses such as SIRV2 (Sulfolobus islandicus rod-shaped virus) have revealed an unusual lysis mechanism that involves the formation of pyramidal egress structures on the host cell surface. To expand understanding of the infection cycle of SIRV2, we aimed to functionally characterize gp1, which is a SIRV2 gene with unknown function. The SIRV2_Gp1 protein is highly expressed during early stages of infection and it is the only protein that is encoded twice on the viral genome. It harbours a helix-turn-helix motif and was therefore hypothesized to bind DNA. The DNA-binding behavior of SIRV2_Gp1 was characterized with electrophoretic mobility shift assays and atomic force microscopy. We provide evidence that the protein interacts with DNA and that it forms large aggregates, thereby causing extreme condensation of the DNA. Furthermore, the N-terminal domain of the protein mediates toxicity to the viral host Sulfolobus. Our findings may lead to biotechnological applications, such as the development of a toxic peptide for the containment of pathogenic bacteria, and add to our understanding of the Rudiviral infection cycle. ispartof: VIRUSES-BASEL vol:9 issue:7 ispartof: location:Switzerland status: published |
| Databáze: | OpenAIRE |
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