Phosphorylation of serine residues in the N-terminal domains of eukaryotic type I topoisomerases

Krzysztof Staron, D. Scott Samuels

Research output: Contribution to journalArticlepeer-review

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 languageEnglish
Pages (from-to)157-161
Number of pages5
JournalMolecular Biology Reports
Volume25
Issue number3
DOIs
StatePublished - Jul 1998

Keywords

  • DNA topoisomerase I
  • N-terminal domain
  • Serine phosphorylation

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