SpoIIIE protein achieves directional DNA translocation through allosteric regulation of ATPase activity by an accessory domain.

ABSTRACT: Bacterial chromosome segregation utilizes highly conserved directional translocases of the SpoIIIE/FtsK family. These proteins employ an accessory DNA-binding domain (γ) to dictate directionality of DNA transport. It remains unclear how the interaction of γ with specific recognition sequences coordinates directional DNA translocation. We demonstrate that the γ domain of SpoIIIE inhibits ATPase activity of the motor domain in the absence of DNA but stimulates ATPase activity through sequence-specific DNA recognition. Furthermore, we observe that communication between γ subunits is necessary for both regulatory roles. Consistent with these findings, the γ domain is necessary for robust DNA transport along the length of the chromosome in vivo. Together, our data reveal that directional activa

SUBMITTER: Besprozvannaya M 

PROVIDER: S-EPMC3789994 | biostudies-literature | 2013 Oct

REPOSITORIES: biostudies-literature