Nuclear localization of 68 kDa calmodulin-binding protein is associated with the onset of DNA replication.

Autor: Subramanyam C; Department of Obstetrics and Gynecology, University of Virginia Diabetes Center, Charlottesville 22906., Honn SC, Reed WC, Reddy GP
Jazyk: angličtina
Zdroj: Journal of cellular physiology [J Cell Physiol] 1990 Sep; Vol. 144 (3), pp. 423-8.
DOI: 10.1002/jcp.1041440309
Abstrakt: In Chinese hamster embryo fibroblast cells, an increase in intracellular calmodulin levels coincided with the nuclear localization of a calmodulin-binding protein of about 68 kDa as the cells progressed from G1 to S phase. When cells were limited from entering into S phase, by omitting insulin a defined medium, intracellular CaM levels did not increase and the 68 kDa calmodulin-binding protein was completely absent from the nuclei. Corresponding to the nuclear localization of calmodulin and the 68 kDa calmodulin-binding protein in S phase cells, there was a dramatic increase in DNA polymerase and thymidine kinase activities in the nuclei of S phase cells as compared to G1 phase cells. In addition, the 68 kDa calmodulin-binding protein, along with calmodulin, is observed to be an integral component of replitase complex responsible for nuclear DNA replication in S phase cells. These observations point to the association of calmodulin and calmodulin-binding protein(s) with the replication machinery responsible for nuclear DNA replication during S phase. A possible regulatory role of these proteins in the onset of DNA replication and cell proliferation is discussed.
Databáze: MEDLINE