Phosphorylation of serine residues in the N-terminal domains of eukaryotic type I topoisomerases.
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.
Institute of Biochemistry, Warsaw University, Poland.
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Samuels
D000818:Animals; D047390:Casein Kinase II; D002855:Chromatography, Thin Layer; D016384:Consensus Sequence; D004264:DNA Topoisomerases, Type I / Q000737:chemistry* / Q000378:metabolism; D005057:Eukaryotic Cells / Q000201:enzymology; D006801:Humans; D007526:Isoelectric Point; D010449:Peptide Mapping; D010766:Phosphorylation; D010768:Phosphoserine / Q000032:analysis* / Q000378:metabolism; D011493:Protein Kinase C; D017346:Protein Serine-Threonine Kinases; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid; D012694:Serine / Q000032:analysis; D014357:Trypsin
D010768:Phosphoserine; D012694:Serine; D047390:Casein Kinase II; D017346:Protein Serine-Threonine Kinases; D011493:Protein Kinase C; D014357:Trypsin; D004264:DNA Topoisomerases, Type I