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Mediator structure and rearrangements required for holoenzyme formation.

These activity differences are explained by the fact that CaMKII functions as a dodecamer, and the linker length determines the compactness and thus the substrate accessibility of the holoenzyme—enzymes with long linkers have higher activity.

Conceivably, such a phenomenon could reflect migration to ‘transcription factories’—preassembled nuclear subcompartments that contain RNA polymerase II holoenzyme.