Remodeling of RecG helicase at the DNA replication fork by SSB protein

Zhiqiang Sun, Hui Yin Tan, Piero R. Bianco, Yuri L Lyubchenko

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The RecG DNA helicase a key player in stalled replication fork rescue. The single-stranded DNA binding protein (SSB) participates in this process, but its role in the interaction of RecG with the fork remains unclear. We used atomic force microscopy (AFM) to visualize the interaction of RecG with a fork DNA in the presence of SSB. We discovered that SSB enhances RecG loading efficiency onto the DNA fork by threefold. Additionally, SSB interacts with RecG leading to the RecG remodeling. As a result, RecG separates from the fork, but remains bound to the DNA duplex. Moreover, in this new binding mode RecG is capable of translocation along the parental duplex DNA. We propose a model of RecG interaction with the replication fork involving two RecG binding modes. SSB plays the role of a remodeling factor defining the mode of RecG binding to the fork mediated by the SSB C-terminus. In the translocating mode, RecG remains in the vicinity of the fork and is capable of initiating the fork regression. Our results afford novel mechanistic insights into RecG interaction with the replication fork and provide the basis for further structural studies.

Original languageEnglish (US)
Article number9625
JournalScientific reports
Volume5
DOIs
StatePublished - Apr 29 2015

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DNA Replication
DNA
Proteins
DNA Helicases
Atomic Force Microscopy
DNA-Binding Proteins

ASJC Scopus subject areas

  • General

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Remodeling of RecG helicase at the DNA replication fork by SSB protein. / Sun, Zhiqiang; Tan, Hui Yin; Bianco, Piero R.; Lyubchenko, Yuri L.

In: Scientific reports, Vol. 5, 9625, 29.04.2015.

Research output: Contribution to journalArticle

Sun, Zhiqiang ; Tan, Hui Yin ; Bianco, Piero R. ; Lyubchenko, Yuri L. / Remodeling of RecG helicase at the DNA replication fork by SSB protein. In: Scientific reports. 2015 ; Vol. 5.
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