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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/39059
Title: In Vivo Assembly of Phage ϕ29 Replication Protein p1 into Membrane-associated Multimeric Structures
Authors: Serrano-Heras, Gemma; Salas, Margarita; Bravo García, Alicia
Issue Date: 6-Aug-2003
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Journal of Biological Chemistry 278: 40771-40777 (2003)
Abstract: The mechanisms underlying compartmentalization of prokaryotic DNA replication are largely unknown. In the case of the Bacillus subtilis phage ϕ29, the viral protein p1 enhances the rate of in vivo viral DNA replication. Previous work showed that p1 generates highly ordered structures in vitro. We now show that protein p1, like integral membrane proteins, has an amphiphilic nature. Furthermore, immunoelectron microscopy studies reveal that p1 has a peripheral subcellular location. By combining in vivo chemical cross-linking and cell fractionation techniques, we also demonstrate that p1 assembles in infected cells into multimeric structures that are associated with the bacterial membrane. These structures exist both during viral DNA replication and when ϕ29 DNA synthesis is blocked due to the lack of viral replisome components. In addition, protein p1 encoded by plasmid generates membrane-associated multimers and supports DNA replication of a p1-lacking mutant phage, suggesting that the pre-assembled structures are functional. We propose that a phage structure assembled on the cell membrane provides a specific site for ϕ29 DNA replication.
Publisher version (URL): http://dx.doi.org/10.1074/jbc.M306935200
URI: http://hdl.handle.net/10261/39059
DOI: 10.1074/jbc.M306935200
ISSN: 0021-9258
E-ISSN: 1083-351X
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