PerspectiveMolecular Biology

An unexpected cofactor

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Science  29 Nov 2019:
Vol. 366, Issue 6469, pp. 1072-1073
DOI: 10.1126/science.aaz8632

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Summary

Accurate chromosome segregation is essential for organisms in all kingdoms of life. In bacteria, which do not compartmentalize their chromosomes into nuclei or undergo mitosis, this process is as important as it is in eukaryotes. Bacterial chromosomes typically contain centromere partition sites (parS). Centromeres are DNA sites necessary for segregation, which is generally called “partition” in bacteria. The parS sites are bound by centromere-binding ParB (partition protein B) proteins. On page 1129 of this issue, Soh et al. (1) report the unexpected and remarkable discovery that ParB proteins use cytidine triphosphate (CTP) as a cofactor when they assemble partition complexes, and that ParB is an enzyme capable of CTP hydrolysis in addition to its DNA binding activities. ParB proteins interact with partition adenosine triphosphatases (ATPases) called ParA and, until the study of Soh et al., ATP was believed to be the only nucleotide cofactor required in this type of partition reaction.

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