Abstract
These studies indicate that SV40T antigen binds the amino terminus of human top1 both in vitro and in vivo. Additional in vitro data suggest that the interaction between these two proteins does not require DNA as an intermediary. Taken together with the finding that the amino terminus of top1 binds the putative helicase nucleolin, these results implicate helicase binding as a general function of the amino terminus of human top1. Binding of top1 by helicases may be important in the management of structural alterations in DNA produced by helicases. The potential importance of helicase-topoisomerase interactions has been highlighted by recent data indicating that the protein defective in Bloom's syndrome is a helicase with a yeast homologue that is known to bind topoisomerases.
Original language | English (US) |
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Pages (from-to) | 253-262 |
Number of pages | 10 |
Journal | Advances in Enzyme Regulation |
Volume | 38 |
Issue number | 1 |
DOIs | |
State | Published - Jul 1998 |
ASJC Scopus subject areas
- Molecular Medicine
- Molecular Biology
- Genetics
- Cancer Research