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Originally published In Press as doi:10.1074/jbc.M204467200 on July 17, 2002

J. Biol. Chem., Vol. 277, Issue 39, 35969-35979, September 27, 2002
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Homologous-pairing Activity of the Bacillus subtilis Bacteriophage SPP1 Replication Protein G35P*

Silvia AyoraDagger §, Riccardo MissichDagger , Pablo MesaDagger , Rudi Lurz, Shixin Yang||, Edward H. Egelman||, and Juan C. AlonsoDagger **

From the Dagger  Departmento de Biotecnología Microbiana, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Campus Universidad Autónoma de Madrid, Madrid 28049, Spain, the § Departamento de Biología Molecular, Universidad Autónoma de Madrid, 28049 Madrid, Spain, the  Max-Planck-Institut für molekulare Genetik, Ihnestrasse 73, D-14195 Berlin, Germany, and the || Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, Virginia 22908

Genetic evidence suggests that the SPP1-encoded gene 35 product (G35P) is essential for phage DNA replication. Purified G35P binds single-strand DNA (ssDNA) and double-strand (dsDNA) and specifically interacts with SPP1-encoded replicative DNA helicase G40P and SSB protein G36P. G35P promotes joint molecule formation between a circular ssDNA and a homologous linear dsDNA with an ssDNA tail. Joint molecule formation requires a metal ion but is independent of a nucleotide cofactor. Joint molecules formed during these reactions contain a displaced linear ssDNA strand. Electron microscopic analysis shows that G35P forms a multimeric ring structure in ssDNA tails of dsDNA molecules and left-handed filaments on ssDNA. G35P promotes strand annealing at the AT-rich region of SPP1 oriL on a supercoiled template. These results altogether are consistent with the hypothesis that the homologous pairing catalyzed by G35P is an integral part of SPP1 DNA replication. The loading of G40P at a D-loop (ori DNA or at any stalled replication fork) by G35P could lead to replication fork reactivation.

* This work was supported by Grants BMC2000-0548 and BIO2001-4342-E from Dirección General de Investigación-Ministerio de Ciencia y Tecnología (DGI-MCYT) and QLRT-2000-00365 from the European Union (to J. C. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

** To whom correspondence should be addressed. Tel.: 34-91-585-4546; Fax: 34-91-585-4506; E-mail. jcalonso@cnb.uam.es.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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