RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair

Katsumi Morimatsu, Stephen C. Kowalczykowski

Research output: Contribution to journalArticle

284 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)1337-1347
Number of pages11
JournalMolecular Cell
Volume11
Issue number5
DOIs
StatePublished - May 1 2003

Fingerprint

Rec A Recombinases
Recombinational DNA Repair
DNA
Proteins
DNA-Binding Proteins
DNA Repair

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 journalArticle

Morimatsu, Katsumi ; Kowalczykowski, Stephen C. / RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange : A universal step of recombinational repair. In: Molecular Cell. 2003 ; Vol. 11, No. 5. pp. 1337-1347.
@article{63955fa21bc44feb9db3cb21457a3599,
title = "RecFOR proteins load RecA protein onto gapped DNA to accelerate DNA strand exchange: A universal step of recombinational repair",
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.",
author = "Katsumi Morimatsu and Kowalczykowski, {Stephen C.}",
year = "2003",
month = "5",
day = "1",
doi = "10.1016/S1097-2765(03)00188-6",
language = "English (US)",
volume = "11",
pages = "1337--1347",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",

}

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 -