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Journal Article

Homologous-pairing Activity of the Bacillus subtilis bacteriophage SPP1 Replication Protein G35P

MPS-Authors

Lurz,  Rudi
Max Planck Society;

Alonso,  Juan C.
Max Planck Society;

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Citation

Ayora, S., Missich, R., Mesa, P., Lurz, R., Yang, S., Egelman, E. H., et al. (2002). Homologous-pairing Activity of the Bacillus subtilis bacteriophage SPP1 Replication Protein G35P. Journal of Biological Chemistry, 277(39), 35969-35979.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-8BA3-9
Abstract
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.