CTP and centromere-like parS-DNA act synergistically and catalytically to activate ParB, which remains activated after leaving parS to tune ParA–ParB and ParB–ParB interaction dynamics for robust ParABS-mediated F-plasmid DNA segregation.

A structural and biochemical approach shows that CTP binding and hydrolysis regulate nucleation, spreading, and recycling of a chromosome segregation protein ParB.

Unique sequence feature requirements for the plasmid centromere pSM19035-parS for ParA_pSM-ATPase activation byribbon-helix-helix-ParB_pSM, a non-CTPase centromere-binding protein, evince complex interaction gymnastics among the three reaction components necessary for plasmid partition, which is distinct from ParABS-systems involving helix-turn-helix-ParB-CTPases.

Single-molecule methods reveal that cytidine triphosphate promotes DNA condensation specifically at bacterial centromeres by facilitating one-dimensional diffusion of ParB from parS sites.

Cryptic alleles affecting embryonic development are widespread in wild C. elegans populations.

A biochemical reconstitution shows that the accumulation of Caulobacter crescentus ParB on DNA requires cytidine triphosphate and a closed DNA substrate in vitro.

In vitro, in vivo and in silico evidence suggests that bacteria exploit intrinsic chromosomal fluctuations to achieve intracellular transport.

The ParABS system positions plasmids precisely within the cell but just below the threshold for oscillatory dynamics.

DNA-bound crystal structures of an essential Xer site-specific recombinase from the bacterium Helicobacter pylori reveal how large conformational changes initiate the untangling of chromosomes upon cell division.

A comprehensive analysis of Tensin3 function in oligodendrogenesis links the fields of transcriptional control in oligodendrocyte lineage cells with morphogenetic changes and integrin signaling mediated cell survival.