Association of calmodulin with isolated nuclei from rat hepatocytes.

Calmodulin plays an important role in regulating cell proliferation and intranuclear processes (J. Biol. Chem. 265: 18595, 1990). Therefore we studied the association of 125I-calmodulin with highly purified rat hepatocyte nuclear preparations which were characterized by marker enzymes and electron microscopy. Steady-state association of 125I-calmodulin was reached within 5 minutes. Half-maximal binding was achieved at approximately 7.1 microM. This association was partially Ca(2+)-dependent, but was not influenced by ATP, GTP or wheat germ agglutinin. Ultrastructural autoradiography showed specific association of 125I-calmodulin with peripheral and non-peripheral heterochromatin, nuclear membranes, and nucleoli. Specific binding (ratio of the grain density of 125I-calmodulin to Na125I) was greatest in the regions of the nucleoli and non-peripheral heterochromatin. The data indicate that exogenous calmodulin can associate with specific nuclear components in an energy-independent and Ca(2+)-dependent manner.