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Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/39055
Title: Bacteriophage Φ29 Early Protein p17: self-association and hetero-association with the viral histone-like protein p6
Authors: Crucitti, Paola; Abril, Ana M.; Salas, Margarita
Issue Date: 11-Dec-2003
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Journal of Biological Chemistry 278: 4906-4911 (2003)
Abstract: Gene 17 of the Bacillus subtilis phage Φ29 is expressed early after infection, and it has been shown to be required at the very beginning of phage replication under conditions of low but not high multiplicity of infection. It has been proposed that, at the beginning of the infection, protein p17 could be recruiting limiting amounts of initiation factors at the viral origins. Once the infection process is established and the replication proteins reach optimal concentration, protein p17 becomes dispensable. In this paper we focused, on the one hand, on the study of protein p17 dimerization and the role of a putative coiled-coil region. On the other hand, we focused on its interaction with the viral origin-binding protein p6. Based on our results we propose that protein p17 function is to optimize binding of protein p6 at the viral DNA ends, thus favoring the initiation of replication and negatively modulating its own transcription
Publisher version (URL): http://dx.doi.org/10.1074/jbc.M210289200
URI: http://hdl.handle.net/10261/39055
DOI: 10.1074/jbc.M210289200
ISSN: 0021-9258
E-ISSN: 1083-351X
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