DNA-interacting characteristics of the archaeal rudiviral protein SIRV2_Gp1
Peeters, E; Boon, M; Rollie, C; et al.Willaert, R; Voet, M; White, MF; Prangishvili, D; Lavigne, R; Quax, TEF
Date: 1 July 2017
Article
Journal
Viruses
Publisher
MDPI
Publisher DOI
Abstract
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 ...
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.
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