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Papers In Press, published online ahead of print December 10, 2001
J. Biol. Chem, 10.1074/jbc.M109312200
Submitted on September 26, 2001
Revised on November 19, 2001
Accepted on December 10, 2001

The Bacillus subtilis phage phi 29 protein p16.7, involved in phi 29 DNA replication, is a membrane-localized single-stranded DNA binding protein

Alejandro Serna-Rico, Margarita Salas, and Wilfried J.J. Meijer

Centro de Biologia Molecular, Universidad Autonoma Madrid, Madrid, Madrid 28049

Corresponding Author: msalas{at}cbm.uam.es

The functional role of the phi 29-encoded integral membrane protein p16.7 in phage DNA replication was studied using a soluble variant, p16.7A, lacking the N-terminal membrane-spanning domain. Due to the protein-primed mechanism of DNA replication, the bacteriophage phi 29 replication intermediates contain long stretches of ssDNA. Protein p16.7A was found to be an ssDNA binding protein. In addition, by direct and functional analysis we show that protein p16.7A binds to the stretches of ssDNA of the phi 29 DNA replication intermediates. Properties of protein p16.7A were compared with those of the phi 29-encoded SSB protein p5. The results obtained show that both proteins have different, non-overlapping functions. The likely role of p16.7 in attaching phi 29 DNA replication intermediates to the membrane of the infected cell is discussed. Homologues of gene 16.7 are present in phi 29-related phages suggesting that the proposed role of p16.7 is conserved in this family of phages.


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