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

Ayora, Silvia; Missich, Riccardo; Mesa, Pablo; Lurz, Rudi; Yang, Shixin; Egelman, Edward H.; Alonso, Juan C.

Item

ITEM ACTIONSEXPORT

Add to Basket

Local TagsRelease HistoryDetailsSummary

Released

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;

External Resource

No external resources are shared

Fulltext (restricted access)

There are currently no full texts shared for your IP range.

Fulltext (public)

There are no public fulltexts stored in PuRe

Supplementary Material (public)

There is no public supplementary material available

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: https://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.