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|Título :||A uracil-DNA glycosylase inhibitor encoded by a non-uracil containing viral DNA|
|Autor :||Serrano-Heras, Gemma, Salas, Margarita, Bravo García, Alicia|
|Fecha de publicación :||18-Jan-2006|
|Editor:||American Society for Biochemistry and Molecular Biology|
|Resumen:||Uracil-DNA glycosylase (UDG) is an enzyme involved in the base excision repair pathway. It specifically removes uracil from both single-stranded and double-stranded DNA. The genome of the Bacillus subtilis phage ϕ29 is a linear double-stranded DNA with a terminal protein covalently linked at each 5′-end. Replication of ϕ29 DNA starts by a protein-priming mechanism and generates intermediates that have long stretches of single-stranded DNA. By using in vivo chemical cross-linking and affinity chromatography techniques, we found that UDG is a cellular target for the early viral protein p56. Addition of purified protein p56 to B. subtilis extracts inhibited the endogenous UDG activity. Moreover, extracts from ϕ29-infected cells were deficient in UDG activity. We suggested that inhibition of the cellular UDG is a defense mechanism developed by ϕ29 to prevent the action of the base excision repair pathway if uracil residues arise in their replicative intermediates. Protein p56 is the first example of a UDG inhibitor encoded by a non-uracil-containing viral DNA.|
|Versión del editor:||http://dx.doi.org/10.1074/jbc.M511152200|
|Citación :||Journal of Biological Chemistry 281: 7068-7074 (2006)|
|Appears in Collections:||(CBM) Artículos|
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