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

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.

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Item Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8BA3-9 Version Permalink: https://hdl.handle.net/11858/00-001M-0000-0010-8BA4-7
Genre: Journal Article

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 Creators:
Ayora, Silvia, Author
Missich, Riccardo, Author
Mesa, Pablo, Author
Lurz, Rudi1, Author
Yang, Shixin, Author
Egelman, Edward H., Author
Alonso, Juan C.1, Author
Affiliations:
1Max Planck Society, ou_persistent13              

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 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.

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Language(s): eng - English
 Dates: 2002-09-27
 Publication Status: Issued
 Pages: -
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 Table of Contents: -
 Rev. Type: -
 Identifiers: eDoc: 24199
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 277 (39) Sequence Number: - Start / End Page: 35969 - 35979 Identifier: -