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 |
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Pages (from-to) | 157-161 |
Number of pages | 5 |
Journal | Molecular Biology Reports |
Volume | 25 |
Issue number | 3 |
DOIs | |
State | Published - Jul 1998 |
Keywords
- DNA topoisomerase I
- N-terminal domain
- Serine phosphorylation