Abstract
Genetic evidence suggests that the RecF, RecO, and RecR (RecFOR) proteins participate in a common step of DNA recombination and repair, yet the biochemical event requiring collaboration of all three proteins is unknown. Here, we show that the concerted action of the RecFOR complex directs the loading of RecA protein specifically onto gapped DNA that is coated with single-stranded DNA binding (SSB) protein, thereby accelerating DNA strand exchange. The RecFOR complex recognizes the junction between the ssDNA and dsDNA regions and requires a base-paired 5′ terminus at the junction. Thus, the RecFOR complex is a structure-specific mediator that targets recombinational repair to ssDNA-dsDNA junctions. This reaction reconstitutes the initial steps of recombinational gapped DNA repair and uncovers an event also common to the repair of ssDNA-tailed intermediates of dsDNA-break repair. We propose that the behavior of the RecFOR proteins is mimicked by functional counterparts that exist in all organisms.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 1337-1347 |
| Number of pages | 11 |
| Journal | Molecular Cell |
| Volume | 11 |
| Issue number | 5 |
| DOIs | |
| State | Published - May 1 2003 |
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ASJC Scopus subject areas
- Molecular Biology
Cite this
RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange : A universal step of recombinational repair. / Morimatsu, Katsumi; Kowalczykowski, Stephen C.
In: Molecular Cell, Vol. 11, No. 5, 01.05.2003, p. 1337-1347.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange
T2 - A universal step of recombinational repair
AU - Morimatsu, Katsumi
AU - Kowalczykowski, Stephen C.
PY - 2003/5/1
Y1 - 2003/5/1
N2 - Genetic evidence suggests that the RecF, RecO, and RecR (RecFOR) proteins participate in a common step of DNA recombination and repair, yet the biochemical event requiring collaboration of all three proteins is unknown. Here, we show that the concerted action of the RecFOR complex directs the loading of RecA protein specifically onto gapped DNA that is coated with single-stranded DNA binding (SSB) protein, thereby accelerating DNA strand exchange. The RecFOR complex recognizes the junction between the ssDNA and dsDNA regions and requires a base-paired 5′ terminus at the junction. Thus, the RecFOR complex is a structure-specific mediator that targets recombinational repair to ssDNA-dsDNA junctions. This reaction reconstitutes the initial steps of recombinational gapped DNA repair and uncovers an event also common to the repair of ssDNA-tailed intermediates of dsDNA-break repair. We propose that the behavior of the RecFOR proteins is mimicked by functional counterparts that exist in all organisms.
AB - Genetic evidence suggests that the RecF, RecO, and RecR (RecFOR) proteins participate in a common step of DNA recombination and repair, yet the biochemical event requiring collaboration of all three proteins is unknown. Here, we show that the concerted action of the RecFOR complex directs the loading of RecA protein specifically onto gapped DNA that is coated with single-stranded DNA binding (SSB) protein, thereby accelerating DNA strand exchange. The RecFOR complex recognizes the junction between the ssDNA and dsDNA regions and requires a base-paired 5′ terminus at the junction. Thus, the RecFOR complex is a structure-specific mediator that targets recombinational repair to ssDNA-dsDNA junctions. This reaction reconstitutes the initial steps of recombinational gapped DNA repair and uncovers an event also common to the repair of ssDNA-tailed intermediates of dsDNA-break repair. We propose that the behavior of the RecFOR proteins is mimicked by functional counterparts that exist in all organisms.
UR - http://www.scopus.com/inward/record.url?scp=0038392868&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0038392868&partnerID=8YFLogxK
U2 - 10.1016/S1097-2765(03)00188-6
DO - 10.1016/S1097-2765(03)00188-6
M3 - Article
C2 - 12769856
AN - SCOPUS:0038392868
VL - 11
SP - 1337
EP - 1347
JO - Molecular Cell
JF - Molecular Cell
SN - 1097-2765
IS - 5
ER -