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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/39421
Title: The integral membrane protein p16.7 organizes in vivo 29 DNA replication through interaction with both the terminal protein and ssDNA
Authors: Serna-Rico, Alejandro; Muñoz-Espín, D.; Villar, Laurentino; Salas, Margarita; Meijer, Wilfried J. J.
Keywords: Bacillus subtilis
Bacteriophage Ψ29
In vivo DNA replication
ssDNA binding
Issue Date: 1-May-2007
Publisher: Nature Publishing Group
Citation: Embo Journal 26: 3494 - 3505 (2007)
Abstract: Remarkably little is known about the in vivo organization of membrane-associated prokaryotic DNA replication or the proteins involved. We have studied this fundamental process using the Bacillus subtilis phage 29 as a model system. Previously, we demonstrated that the 29-encoded dimeric integral membrane protein p16.7 binds to ssDNA and is involved in the organization of membrane-associated 29 DNA replication. Here we demonstrate that p16.7 forms multimers, both in vitro and in vivo, and interacts with the 29 terminal protein. In addition, we show that in vitro multimerization is enhanced in the presence of ssDNA and that the C-terminal region of p16.7 is required for multimerization but not for ssDNA binding or interaction with the terminal protein. Moreover, we provide evidence that the ability of p16.7 to form multimers is crucial for its ssDNA-binding mode. These and previous results indicate that p16.7 encompasses four distinct modules. An integrated model of the structural and functional domains of p16.7 in relation to the organization of in vivo 29 DNA replication is presented.
Publisher version (URL): http://dx.doi.org/10.1093/emboj/cdg221
URI: http://hdl.handle.net/10261/39421
ISSN: 0261-4189
DOI: 10.1093/emboj/cdg221
E-ISSN: 1460-2075
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