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Nucleic Acids Research Advance Access originally published online on August 13, 2007
Nucleic Acids Research 2007 35(16):5393-5401; doi:10.1093/nar/gkm584
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Nucleic Acids Research, 2007, Vol. 35, No. 16 5393-5401
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

Protein p56 from the Bacillus subtilis phage {phi}29 inhibits DNA-binding ability of uracil-DNA glycosylase

Gemma Serrano-Heras1, José A. Ruiz-Masó2, Gloria del Solar2, Manuel Espinosa2, Alicia Bravo2 and Margarita Salas1,*

1Instituto de Biología Molecular ‘Eladio Viñuela’ (CSIC), Centro de Biología Molecular ‘Severo Ochoa’ (CSIC-UAM), Universidad Autónoma, Cantoblanco, 28049 Madrid and 2Centro de Investigaciones Biológicas (CSIC), Ramiro de Maeztu 9, 28040 Madrid, Spain

*To whom correspondence should be addressed. Tel: +34 91 497 8435; Fax: +34 91 497 8490; Email: msalas{at}cbm.uam.es

Received April 27, 2007. Revised July 16, 2007. Accepted July 17, 2007.

Protein p56 (56 amino acids) from the Bacillus subtilis phage {phi}29 inactivates the host uracil-DNA glycosylase (UDG), an enzyme involved in the base excision repair pathway. At present, p56 is the only known example of a UDG inhibitor encoded by a non-uracil containing viral DNA. Using analytical ultracentrifugation methods, we found that protein p56 formed dimers at physiological concentrations. In addition, circular dichroism spectroscopic analyses revealed that protein p56 had a high content of ß-strands (around 40%). To understand the mechanism underlying UDG inhibition by p56, we carried out in vitro experiments using the Escherichia coli UDG enzyme. The highly acidic protein p56 was able to compete with DNA for binding to UDG. Moreover, the interaction between p56 and UDG blocked DNA binding by UDG. We also demonstrated that Ugi, a protein that interacts with the DNA-binding domain of UDG, was able to replace protein p56 previously bound to the UDG enzyme. These results suggest that protein p56 could be a novel naturally occurring DNA mimicry.


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Home page
 Proc. Natl. Acad. Sci. USAHome page
G. Serrano-Heras, A. Bravo, and M. Salas
Inaugural Article: Phage {varphi}29 protein p56 prevents viral DNA replication impairment caused by uracil excision activity of uracil-DNA glycosylase
PNAS, December 9, 2008; 105(49): 19044 - 19049.
[Abstract] [Full Text] [PDF]


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