Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 27, Issue 1, Pages 71-+Publisher
NATURE PORTFOLIO
DOI: 10.1038/s41594-019-0355-2
Keywords
-
Funding
- Wellcome Trust
- MRC
- Medical Research Council [MR/N009258/1]
- BBSRC
- MRC [MR/N009258/1] Funding Source: UKRI
Ask authors/readers for more resources
The RecBCD complex plays key roles in phage DNA degradation, CRISPR array acquisition (adaptation) and host DNA repair. The switch between these roles is regulated by a DNA sequence called Chi. We report cryo-EM structures of the Escherichia coli RecBCD complex bound to several different DNA forks containing a Chi sequence, including one in which Chi is recognized and others in which it is not. The Chi-recognized structure shows conformational changes in regions of the protein that contact Chi and reveals a tortuous path taken by the DNA. Sequence specificity arises from interactions with both the RecC subunit and the sequence itself. These structures provide molecular details for how Chi is recognized and insights into the changes that occur in response to Chi binding that switch RecBCD from bacteriophage destruction and CRISPR spacer acquisition to constructive host DNA repair. Cryo-EM structures of E. coli RecBCD complex with different DNA fork templates containing a Chi sequence reveal the conformational changes upon Chi recognition.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available