Abstract
Biochemistry The bacterial DNA parS centromere recruits the ParB protein to the bacterial chromosome. Soh et al. found that the widespread family of ParB proteins not only bind DNA but also bind and hydrolyze cytidine triphosphate (CTP) (see the Perspective by Funnell). ParB CTP hydrolysis is stimulated by parS and regulates the spreading of ParB protein to the parS flanking regions, which is crucial for organizing the bacterial chromosome. The cytidine triphosphatase domain is conserved in a large variety of protein sequences, suggesting its potential roles in other cellular processes. Science , this issue p. [1129][1]; see also p. [1072][2] [1]: /lookup/doi/10.1126/science.aay3965 [2]: /lookup/doi/10.1126/science.aaz8632
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callDisclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
