Homologous pairing between nucleosome cores on a linear duplex DNA and nucleoprotein filaments of RecA protein-single stranded DNA

Biochimie ◽  
1991 ◽  
Vol 73 (2-3) ◽  
pp. 187-190 ◽  
Author(s):  
K. Muniyappa ◽  
J. Ramdas ◽  
E. Mythili ◽  
S. Galande
1980 ◽  
Vol 77 (7) ◽  
pp. 3962-3966 ◽  
Author(s):  
E. Cassuto ◽  
S. C. West ◽  
J. Mursalim ◽  
S. Conlon ◽  
P. Howard-Flanders

Nature ◽  
1979 ◽  
Vol 281 (5728) ◽  
pp. 191-195 ◽  
Author(s):  
Richard P. Cunningham ◽  
Takehiko Shibata ◽  
Chanchal DasGupta ◽  
Charles M. Radding

1981 ◽  
Vol 9 (16) ◽  
pp. 4201-4210 ◽  
Author(s):  
Era Cassuto ◽  
Stephen C. West ◽  
Jill Podell ◽  
Paul Howard-Flanders

2012 ◽  
Vol 287 (42) ◽  
pp. 35621-35630 ◽  
Author(s):  
Katsumi Morimatsu ◽  
Yun Wu ◽  
Stephen C. Kowalczykowski

The repair of single-stranded gaps in duplex DNA by homologous recombination requires the proteins of the RecF pathway. The assembly of RecA protein onto gapped DNA (gDNA) that is complexed with the single-stranded DNA-binding protein is accelerated by the RecF, RecO, and RecR (RecFOR) proteins. Here, we show the RecFOR proteins specifically target RecA protein to gDNA even in the presence of a thousand-fold excess of single-stranded DNA (ssDNA). The binding constant of RecF protein, in the presence of the RecOR proteins, to the junction of ssDNA and dsDNA within a gap is 1–2 nm, suggesting that a few RecF molecules in the cell are sufficient to recognize gDNA. We also found that the nucleation of a RecA filament on gDNA in the presence of the RecFOR proteins occurs at a faster rate than filament elongation, resulting in a RecA nucleoprotein filament on ssDNA for 1000–2000 nucleotides downstream (5′ → 3′) of the junction with duplex DNA. Thus, RecA loading by RecFOR is localized to a region close to a junction. RecFOR proteins also recognize RNA at the 5′-end of an RNA-DNA junction within an ssDNA gap, which is compatible with their role in the repair of lagging strand gaps at stalled replication forks.


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