Reference Report
| Reference | |||
|---|---|---|---|
| Citation | Corbett, A.H., Fernald, A.W., Osheroff, N. (1993). Protein kinase C modulates the catalytic activity of topoisomerase II by enhancing the rate of ATP hydrolysis: evidence for a common mechanism of regulation by phosphorylation. Biochemistry 32(8): 2090--2097. (Export to RIS) | ||
| FlyBase ID | FBrf0057826 | ||
| Publication Type | Research paper | ||
| PubMed ID | 8383533 | ||
| PubMed Abstract | The catalytic activity of topoisomerase II is stimulated approximately 2-3-fold following phosphorylation by either casein kinase II or protein kinase C. A previous study [Corbett, A. H., DeVore, R. F., & Osheroff, N. (1992) J. Biol. Chem. 267, 20513-20518] demonstrated that casein kinase II regulates the activity of topoisomerase II by specifically enhancing the ability of the enzyme to hydrolyze its ATP cofactor. To determine whether other protein kinases use a similar mechanism to activate the enzyme, the effects of protein kinase C mediated phosphorylation on the individual steps of the topoisomerase II catalytic cycle were assessed. Modification stimulated rates of enzyme-mediated ATP hydrolysis approximately 2.7-fold, but had no effect on any reaction that preceded this step, including enzyme.DNA binding, pre- or poststrand passage DNA cleavage/religation, or the double-stranded DNA strand passage event. Furthermore, the activation of ATP hydrolysis was reversed following treatment of phosphorylated topoisomerase II with alkaline phosphatase. As determined by partial proteolytic mapping, the site(s) of protein kinase C modification was (were) localized to the 350 amino acid C-terminal regulatory domain of topoisomerase II within approximately 50 amino acids of the site(s) phosphorylated by casein kinase II. Finally, while protein kinase C and casein kinase II were able to modify the enzyme simultaneously, rates of ATP hydrolysis for doubly-modified topoisomerase II were comparable to those observed for the enzyme following phosphorylation by either individual kinase.(ABSTRACT TRUNCATED AT 250 WORDS) | ||
| DOI | |||
| Related Publication(s) | |||
Recent Updates
|
|||
| Description |
What does this section display?
This section contains items that were added to this record for each release.
It currently only tracks new links between this FlyBase report and other
FlyBase data classes (e.g. genes, references, stocks) or controlled
vocabulary terms (e.g. GO, anatomy terms).
What does this section not display?
This section does not currently display links that were removed or gene model changes.
|
||
| Update Feed |
Click the icon below to subscribe to this FlyBase record and receive updates automatically through your
feed reader.
|
||
| FB2013_03 | |||
| FB2013_02 | |||
| All updates | Click here to see a list of all updates to this record from FB2010_08 and on. | ||
Associated Information
|
|||
| Comments | |||
| Associated Files | |||
Other Information
|
|||
| Secondary IDs | |||
| Language of Publication | English | ||
| Additional Languages of Abstract | |||
| Also Published As | |||
Parent Publication
|
|||
| Publication Type | Journal | ||
| Abbreviation | Biochemistry | ||
| Title | Biochemistry | ||
| Publication Year | 1962- | ||
| ISBN/ISSN | 0006-2960 | ||
Data from Reference
|
|||
Genes (4)
|
|||
Recent Updates