Abstract
Eukaryotic topoisomerase I polypeptides can be partitioned into four structural domains. The function of the N-terminal domain, which is a target for serine-specific phosphorylation, has not been fully defined. The number of serine residues in the N-terminal domain of topoisomerase I from different species is inversely proportional to the number of charged amino acids in this region of the protein. The significance of this correlation is discussed in terms of a possible role for serine-specific phosphorylation in the activity of the enzyme.
| Original language | English |
|---|---|
| Pages (from-to) | 157-161 |
| Number of pages | 5 |
| Journal | Molecular Biology Reports |
| Volume | 25 |
| Issue number | 3 |
| DOIs | |
| State | Published - Jul 1998 |
Funding
This work was supported by M. Sklodowska-Curie Fund Grant MEN/NSF 96-274. DSS was supported in part by a National Research Service Award from the National Cancer Institute (CA-09213). We thank Mike Minnick for assistance with photography.
| Funder number |
|---|
| T32CA009213 |
Keywords
- DNA topoisomerase I
- N-terminal domain
- Serine phosphorylation
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