Self-organization of parS centromeres by the ParB CTP hydrolase

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Science  29 Nov 2019:
Vol. 366, Issue 6469, pp. 1129-1133
DOI: 10.1126/science.aay3965

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CTP hydrolysis organizes chromosomes

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; see also p. 1072

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