Biochemical studies have suggested that some actin and myosin may be present in the nucleus. This raises the possibility that heterochromatin condensation might be the result of an actin-myosin rigour type complex. Since ATP dissociates actin and myosin, this possibility could be examined by determining the effect of ATP on heterochromatin condensation. Thin-section electron microscopy showed large amounts of condensed constitutive heterochromatin in the kidney nuclei and somewhat less in the liver nuclei of the kangaroo rat, Dipidomys ordii. Surprisingly, there were some nuclei in the brain which contained no condensed heterochromatin despite the fact that this genome is composed of 50% satellite DNA. Although washing kidney nuclei with solutions of 10 mM Tris-ATP caused marked decondensation of the heterochromatin, when they were washed with Mg-ATP the heterochromatin was more condensed than in the controls. This suggests the decondensation by Tris-ATP is due to its ability to chelate divalent cations and provides no support for condensation of heterochromatin being the result of myosin-actin interaction. Despite being decondensed, the chromatin fibres of heterochromatin were distinct from those of euchromatin. The heterochromatin formed rod-like 19-5 nm fibres, the euchromatin formed random coils of 11-0-nm fibres.

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