Journal
NUCLEIC ACIDS RESEARCH
Volume 39, Issue 22, Pages 9681-9694Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkr680
Keywords
-
Categories
Funding
- VolkswagenStiftung
- Swiss National Science Foundation
- NCCR Nanoscale Sciences
- University of Basel
Ask authors/readers for more resources
DNA gyrase catalyzes ATP-dependent negative supercoiling of DNA in a strand passage mechanism. A double-stranded segment of DNA, the T-segment, is passed through the gap in a transiently cleaved G-segment by coordinated closing and opening of three protein interfaces in gyrase. T-segment capture is thought to be guided by the C-terminal domains of the GyrA subunit of gyrase that wrap DNA around their perimeter and cause a DNA-crossing with a positive handedness. We show here that the C-terminal domains are in a downward-facing orientation in the absence of DNA, but swing up and rotate away from the gyrase body when DNA binds. The upward movement of the C-terminal domains is an early event in the catalytic cycle of gyrase that is triggered by binding of a G-segment, and first contacts of the DNA with the C-terminal domains, and contributes to T-segment capture and subsequent strand passage.
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