scholarly journals Interaction RecA -protein with nuclei chromatin (the cytological aspect)

1991 ◽  
Vol 7 (3) ◽  
pp. 54-59 ◽  
Author(s):  
S. P. Shpilevaya ◽  
I. E. Kostetsky ◽  
T. V. Stolar ◽  
L. L. Likhachova ◽  
L. G. Zharova ◽  
...  
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.


1989 ◽  
Vol 264 (29) ◽  
pp. 17395-17400 ◽  
Author(s):  
J Ramdas ◽  
E Mythili ◽  
K Muniyappa

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