Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo.

Journal Article (Journal Article)

The decatenation activity of DNA topoisomerase II is essential for viability as eukaryotic cells traverse mitosis. Phosphorylation has been shown to stimulate topoisomerase II activity in vitro. Here we show that topoisomerase II is a phosphoprotein in yeast and that the level of incorporated phosphate is significantly higher at mitosis than in G1. Comparison of tryptic phosphopeptide maps reveals that the major phosphorylation sites in vivo are targets for casein kinase II. Incorporation of phosphate into topoisomerase II is nearly undetectable at the non-permissive temperature in a conditional casein kinase II mutant. The sites modified by casein kinase II are located in the extreme C-terminal domain of topoisomerase II. This domain is absent in prokaryotic and highly divergent among eukaryotic type II topoisomerases, and may serve to regulate functions of topoisomerase II that are unique to eukaryotic cells.

Full Text

Duke Authors

Cited Authors

  • Cardenas, ME; Dang, Q; Glover, CV; Gasser, SM

Published Date

  • May 1992

Published In

Volume / Issue

  • 11 / 5

Start / End Page

  • 1785 - 1796

PubMed ID

  • 1316274

Pubmed Central ID

  • PMC556636

International Standard Serial Number (ISSN)

  • 0261-4189

Digital Object Identifier (DOI)

  • 10.1002/j.1460-2075.1992.tb05230.x


  • eng

Conference Location

  • England