3.4.22.49 cell division cycle 6 Cdc6, a mitotic substrate of polo-like kinase. Cleavage of chesin/Rad21 is much greater in wild-type Cdc6 expressing cells than in GFP and Cdc6-T37V mutant expressing cells 718320 3.4.22.49 cyclinB1 - 732703 3.4.22.49 DNA chromosomal DNA is required as a cofactor for the cleavage of cohesin to occur, and allows separase to selectively cleave only the chromosome-associated cohesin 718177 3.4.22.49 DNA chromosomal DNA is required as a cofactor for the cleavage of cohesin to occur, and allows separase to selectively cleave only the chromosome-associated cohesin. Separase binds to DNA in a sequence nonspecific manner in vitro and associates with the entire length of the mitotic chromosomes 718177 3.4.22.49 imatinib activation of separase proteolytic activity occurs exclusively in BCR-ABL-positive cells during imatinib treatment (0.00025-0.01 mM for 24 h) 732703 3.4.22.49 additional information Cdc20 is essential for mitotic progression 718037 3.4.22.49 additional information most of the budding yeast cohesin is cleaved in anaphase, and this cleavage is stimulated by phosphorylation of the Scc1 subunit by the Plk1 kinase 718177 3.4.22.49 additional information separase can be activated by incubating immunoglobulin G-Sepharose 6 containing ZZ TEV4-separase with anaphase-initiated Xenopus cytostatic factor to degrade its inhibitor securin at room temperature for 1 h 707105 3.4.22.49 additional information separase shows self-cleavage upon activation 664553 3.4.22.49 PP2A - 732703 3.4.22.49 securin - 638862 3.4.22.49 securin activation may be due to separase localization 638862 3.4.22.49 securin securin is required to support separase activity in anaphase 638864 3.4.22.49 securin the central domain of securin has a functionally essential specific sequence that may directly interact with the catalytic region of separase. This central securin domain is unrelated to destruction by polyubiquitination, but essential for the activation of separase 665049 3.4.22.49 securing - 732703 3.4.22.49 securing the motif containing H134 in securing isoform PTTG1 has a strong affinity for separase and is involved in inhibiting it, while another domain(s) in isoform PTTG2 is involved in activating separase and has a weaker affinity for it. Isoform PTTG2 does not interact with separase 732505