RT Journal Article SR Electronic T1 A CTP-dependent gating mechanism enables ParB spreading on DNA in Caulobacter crescentus JF bioRxiv FD Cold Spring Harbor Laboratory SP 816959 DO 10.1101/816959 A1 Adam S. B. Jalal A1 Ngat T. Tran A1 Clare. E. M. Stevenson A1 Afroze Chimthanawala A1 Anjana Badrinarayanan A1 David M. Lawson A1 Tung B. K. Le YR 2021 UL http://biorxiv.org/content/early/2021/05/05/816959.abstract AB Proper chromosome segregation is essential in all living organisms. The ParA-ParB-parS system is widely employed for chromosome segregation in bacteria. Previously, we showed that Caulobacter crescentus ParB requires cytidine triphosphate to escape the nucleation site parS and spread by sliding to the neighboring DNA. Here, we provide the structural basis for this transition from nucleation to spreading by solving co-crystal structures of a C-terminal domain truncated C. crescentus ParB with parS and with a CTP analog. Nucleating ParB is an open clamp, in which parS is captured at the DNA-binding domain (the DNA-gate). Upon binding CTP, the N-terminal domain (NTD) self-dimerizes to close the NTD-gate of the clamp. The DNA-gate also closes, thus driving parS into a compartment between the DNA-gate and the C-terminal domain. CTP hydrolysis and/or the release of hydrolytic products may subsequently re-open the gates. Overall, we suggest a CTP-operated gating mechanism that regulates ParB nucleation and spreading.Competing Interest StatementThe authors have declared no competing interest.