Cyclin A-dependent kinase activity affects chromatin binding of ORC, Cdc6, and MCM in egg extracts of Xenopus laevis. Export

@article{citeulike:4064236, abstract = {The initiation of DNA replication in eukaryotes requires the loading of the origin recognition complex (ORC), Cdc6, and minichromosome maintenance (MCM) proteins onto chromatin to form the preinitiation complex. In Xenopus egg extract, the proteins Orc1, Orc2, Cdc6, and Mcm4 are underphosphorylated in interphase and hyperphosphorylated in metaphase extract. We find that chromatin binding of ORC, Cdc6, and MCM proteins does not require cyclin-dependent kinase activities. High cyclin A-dependent kinase activity inhibits the binding and promotes the release of Xenopus ORC, Cdc6, and MCM from sperm chromatin, but has no effect on chromatin binding of control proteins. Cyclin A together with ORC, Cdc6 and MCM proteins is bound to sperm chromatin in DNA replicating pseudonuclei. In contrast, high cyclin E/cdk2 was not detected on chromatin, but was found soluble in the nucleoplasm. High cyclin E kinase activity allows the binding of Xenopus ORC and Cdc6, but not MCM, to sperm chromatin, even though the kinase does not phosphorylate MCM directly. We conclude that chromatin-bound cyclin A kinase controls DNA replication by protein phosphorylation and chromatin release of Cdc6 and MCM, whereas soluble cyclin E kinase prevents rereplication during the cell cycle by the inhibition of premature MCM chromatin association.}, author = {Findeisen, M. and El-Denary, M. and Kapitza, T. and Graf, R. and Strausfeld, U.}, citeulike-article-id = {4064236}, citeulike-linkout-0 = {http://view.ncbi.nlm.nih.gov/pubmed/10491086}, citeulike-linkout-1 = {http://www.hubmed.org/display.cgi?uids=10491086}, issn = {0014-2956}, journal = {European journal of biochemistry / FEBS}, keywords = {cdc6, cdk, cyclina, dna, mcm, orc, replication}, month = {September}, number = {2}, pages = {415--426}, posted-at = {2009-02-17 08:40:39}, priority = {2}, title = {Cyclin A-dependent kinase activity affects chromatin binding of ORC, Cdc6, and MCM in egg extracts of Xenopus laevis.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/10491086}, volume = {264}, year = {1999} }

TY - JOUR ID - citeulike:4064236 L3 - citeulike-article-id:4064236 N2 - The initiation of DNA replication in eukaryotes requires the loading of the origin recognition complex (ORC), Cdc6, and minichromosome maintenance (MCM) proteins onto chromatin to form the preinitiation complex. In Xenopus egg extract, the proteins Orc1, Orc2, Cdc6, and Mcm4 are underphosphorylated in interphase and hyperphosphorylated in metaphase extract. We find that chromatin binding of ORC, Cdc6, and MCM proteins does not require cyclin-dependent kinase activities. High cyclin A-dependent kinase activity inhibits the binding and promotes the release of Xenopus ORC, Cdc6, and MCM from sperm chromatin, but has no effect on chromatin binding of control proteins. Cyclin A together with ORC, Cdc6 and MCM proteins is bound to sperm chromatin in DNA replicating pseudonuclei. In contrast, high cyclin E/cdk2 was not detected on chromatin, but was found soluble in the nucleoplasm. High cyclin E kinase activity allows the binding of Xenopus ORC and Cdc6, but not MCM, to sperm chromatin, even though the kinase does not phosphorylate MCM directly. We conclude that chromatin-bound cyclin A kinase controls DNA replication by protein phosphorylation and chromatin release of Cdc6 and MCM, whereas soluble cyclin E kinase prevents rereplication during the cell cycle by the inhibition of premature MCM chromatin association. IS - 2 JF - European journal of biochemistry / FEBS SN - 0014-2956 EP - 426 TI - Cyclin A-dependent kinase activity affects chromatin binding of ORC, Cdc6, and MCM in egg extracts of Xenopus laevis. VL - 264 SP - 415 KW - cdc6 KW - cdk KW - cyclina KW - dna KW - mcm KW - orc KW - replication AU - Findeisen, M AU - El-Denary, M AU - Kapitza, T AU - Graf, R AU - Strausfeld, U PY - 1999/09// UR - http://view.ncbi.nlm.nih.gov/pubmed/10491086 ER -