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Originally published In Press as doi:10.1074/jbc.M007855200 on September 25, 2000

J. Biol. Chem., Vol. 275, Issue 51, 40529-40538, December 22, 2000
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The Putative Coiled Coil Domain of the phi 29 Terminal Protein Is a Major Determinant Involved in Recognition of the Origin of Replication*

Alejandro Serna-RicoDagger , Belén Illana§, Margarita Salas, and Wilfried J. J. Meijer

From the Centro de Biología Molecular "Severo Ochoa" (CSIC-UAM), Universidad Autónoma, Canto Blanco, 28049 Madrid, Spain

The linear double-stranded genome of phage phi 29 contains a terminal protein (TP) covalently linked at each 5' DNA end, called parental TP. Initiation of phi 29 DNA replication starts with the recognition of the origins of replication, constituted by the parental TP-containing DNA ends, by a heterodimer containing phi 29 DNA polymerase and primer TP. It has been argued that origin recognition involves protein-protein interactions between parental and primer TP. Analysis of the TP sequence revealed that the region between amino acids 84 and 118 has a high probability to form an amphipatic alpha -helix that could be involved in the interaction between parental and primer TP. Therefore, this TP region may be important for origin recognition. To test this hypothesis we introduced various mutations in the predicted amphipatic alpha -helix and analyzed the functionality of the corresponding purified TP mutants. The results obtained show that the identified putative amphipatic alpha -helix of TP is an important determinant involved in origin recognition.

* This work was supported in part by Research Grant 2R01 GM27242-20 from the National Institutes of Health, PB98-0645 from the Dirección General de Investigación Científica y Técnica, ERBFMX CT97 0125 from the European Economic Community, and an Institutional grant from Fundación Ramón Areces.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.

Dagger Holder of a predoctoral fellowship from Gobierno Vasco.

§ Present address: EnWare S.A. (Grupo ABS), Nuñez de Balboa 51, 28001 Madrid, Spain.

To whom correspondence should be addressed. Tel.: 34-91-397-8435; Fax: 34-91-397-8490; E-mail: Msalas@cbm.uam.es.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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