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 language | English (US) |
|---|---|
| Article number | 9625 |
| Journal | Scientific reports |
| Volume | 5 |
| DOIs | |
| State | Published - Apr 29 2015 |
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ASJC Scopus subject areas
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Cite this
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 journal › Article
}
TY - JOUR
T1 - Remodeling of RecG helicase at the DNA replication fork by SSB protein
AU - Sun, Zhiqiang
AU - Tan, Hui Yin
AU - Bianco, Piero R.
AU - Lyubchenko, Yuri L
PY - 2015/4/29
Y1 - 2015/4/29
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=84928967106&partnerID=8YFLogxK
U2 - 10.1038/srep09625
DO - 10.1038/srep09625
M3 - Article
C2 - 25923319
AN - SCOPUS:84928967106
VL - 5
JO - Scientific Reports
JF - Scientific Reports
SN - 2045-2322
M1 - 9625
ER -