Homologous pairing in genetic recombination: recA protein makes joint molecules of gapped circular DNA and closed circular DNA

Cell ◽  
1980 ◽  
Vol 20 (1) ◽  
pp. 223-235 ◽  
Author(s):  
Richard P. Cunningham ◽  
Chanchal DasGupta ◽  
Takehiko Shibata ◽  
Charles M. Radding
1980 ◽  
Vol 77 (7) ◽  
pp. 3962-3966 ◽  
Author(s):  
E. Cassuto ◽  
S. C. West ◽  
J. Mursalim ◽  
S. Conlon ◽  
P. Howard-Flanders

1994 ◽  
Vol 14 (3) ◽  
pp. 1949-1955
Author(s):  
H Kotani ◽  
E B Kmiec

RecA protein catalyzes the homologous pairing of a single-stranded circular DNA and a linear duplex DNA molecule. When the duplex is packaged into chromatin, formation of homologously paired complexes is blocked. We have established a system for studying the RecA-promoted reaction by using a duplex fragment containing a single-phased nucleosome. Under these conditions there is no reaction leading to formation of joint molecule complexes. However, transcription on the chromatin template activates the formation of complexes. Reaction is dependent on RNA synthesis and DNA sequence homology and proceeds regardless of the direction of transcription.


1981 ◽  
Vol 256 (14) ◽  
pp. 7565-7572
Author(s):  
T. Shibata ◽  
C. DasGupta ◽  
R.P. Cunningham ◽  
J.G. Williams ◽  
L. Osber ◽  
...  

1994 ◽  
Vol 14 (3) ◽  
pp. 1949-1955 ◽  
Author(s):  
H Kotani ◽  
E B Kmiec

RecA protein catalyzes the homologous pairing of a single-stranded circular DNA and a linear duplex DNA molecule. When the duplex is packaged into chromatin, formation of homologously paired complexes is blocked. We have established a system for studying the RecA-promoted reaction by using a duplex fragment containing a single-phased nucleosome. Under these conditions there is no reaction leading to formation of joint molecule complexes. However, transcription on the chromatin template activates the formation of complexes. Reaction is dependent on RNA synthesis and DNA sequence homology and proceeds regardless of the direction of transcription.


1979 ◽  
Vol 76 (10) ◽  
pp. 5100-5104 ◽  
Author(s):  
T. Shibata ◽  
R. P. Cunningham ◽  
C. DasGupta ◽  
C. M. Radding

Author(s):  
E.H. Egelman

The recA protein (38,000MW) of E. coli forms helical polymers which are able, in an ATP-dependent reaction, to mediate the entire genetic recombination process, including the search for homology, homologous pairing, and strand transfer. We have been using computed image analysis of electron micrographs of different recA complexes in an effort to understand the function of this protein in recombination. These filaments typically show poor helical order. We have studied the systematic deviations from helical order (the disorder) present in static images of recA complexes as a means of understanding the dynamics of recA filaments in solution.


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

Author(s):  
E. H. Egelman ◽  
X. Yu

The RecA protein of E. coli has been shown to mediate genetic recombination, regulate its own synthesis, control the expression of other genes, act as a specific protease, form a helical polymer and have an ATPase activity, among other observed properties. The unusual filament formed by the RecA protein on DNA has not previously been shown to exist outside of bacteria. Within this filament, the 36 Å pitch of B-form DNA is extended to about 95 Å, the pitch of the RecA helix. We have now establishedthat similar nucleo-protein complexes are formed by bacteriophage and yeast proteins, and availableevidence suggests that this structure is universal across all of biology, including humans. Thus, understanding the function of the RecA protein will reveal basic mechanisms, in existence inall organisms, that are at the foundation of general genetic recombination and repair.Recombination at this moment is assuming an importance far greater than just pure biology. The association between chromosomal rearrangements and neoplasms has become stronger and stronger, and these rearrangements are most likely products of the recombinatory apparatus of the normal cell. Further, damage to DNA appears to be a major cause of cancer.


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