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| Content Provider | Springer Nature Link |
|---|---|
| Author | Götz, Claudia Scholtes, Petra Prowald, Alexandra Schuster, rbert Nastainczyk, Wolfgang Montenarh, Mathias |
| Copyright Year | 1999 |
| Abstract | p53 is one of the most powerful negative regulators of growth. To manage this in an efficient way it has to interact with a set of different cellular proteins. Most contacts with the cellular environment occur in the N- or the C-terminal domain of the protein. Since we previously found that p53 binds to the regulatory β-subunit of CK2 we now analyzed N- and C-terminal domains of p53 separately for the binding of protein kinase CK2, an enzyme which seems to have a certain importance for proliferation processes. With different overlay assays we could map the binding domain of protein kinase CK2 to a sequence between amino acids 325-344, a region which coincides with the interaction domain of some other p53 binding proteins. We also found that the regulatory β-subunit of protein kinase CK2 binds independent of the catalytic α-subunit to this C-terminal domain of p53. |
| Starting Page | 111 |
| Ending Page | 120 |
| Page Count | 10 |
| File Format | |
| ISSN | 03008177 |
| Journal | Molecular and Cellular Biochemistry |
| Volume Number | 191 |
| Issue Number | 1-2 |
| e-ISSN | 15734919 |
| Language | English |
| Publisher | Kluwer Academic Publishers |
| Publisher Date | 1999-01-01 |
| Publisher Place | Boston |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Cardiology Medical Biochemistry Oncology Biochemistry |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine Clinical Biochemistry Molecular Biology |
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