Residues within the N-terminal Domain of Human Topoisomerase I Play a Direct Role in Relaxation

• Published in: The Journal of biological chemistry Vol. 276; no. 23; pp. 20220 - 20227
• Main Authors: Lisby, Michael, Olesen, Jens R., Skouboe, Camilla, Krogh, Berit O., Straub, Tobias, Boege, Fritz, Velmurugan, Soundarapaudian, Martensen, Pia M., Andersen, Anni H., Jayaram, Makkuni, Westergaard, Ole, Knudsen, Birgitta R.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 08.06.2001; American Society for Biochemistry and Molecular Biology
• Subjects: Catalysis; DNA Topoisomerases, Type I - chemistry; DNA Topoisomerases, Type I - isolation & purification; DNA Topoisomerases, Type I - metabolism; Electrophoresis, Polyacrylamide Gel; Humans; Protein Conformation

All eukaryotic forms of DNA topoisomerase I contain an extensive and highly charged N-terminal domain. This domain contains several nuclear localization sequences and is essential forin vivo function of the enzyme. However, so far no direct function of the N-terminal domain in the in vitrotopoisomer...