Abstract
During the assembly of the bacterial loader-dependent primosome, helicase loader proteins bind to the hexameric helicase ring, deliver it onto the oriC DNA and then dissociate from the complex. Here, to provide a better understanding of this key process, we report the crystal structure of the ∼570-kDa prepriming complex between the Bacillus subtilis loader protein and the Bacillus stearothermophilus helicase, as well as the helicase-binding domain of primase with a molar ratio of 6:6:3 at 7.5 Å resolution. The overall architecture of the complex exhibits a three-layered ring conformation. Moreover, the structure combined with the proposed model suggests that the shift from the 'open-ring' to the 'open-spiral' and then the 'closed-spiral' state of the helicase ring due to the binding of single-stranded DNA may be the cause of the loader release.
| Original language | English (US) |
|---|---|
| Article number | 2495 |
| Journal | Nature communications |
| Volume | 4 |
| DOIs | |
| State | Published - 2013 |
Bibliographical note
Funding Information:We thank the staffs at the Advanced Photon Source beamline 24-ID and at the National Synchrotron Light Source beamline X-29/X-25 for help during data collection. This research was supported by NIH grant GM57510 to T.A.S. T.A.S. is an investigator of the Howard Hughes Medical Institute.