A role for the amino terminus of human topoisomerase I.
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 top 1 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.
Department of Pharmacology, Robert Wood Johnson Medical School, Cancer Institute of New Jersey, University of Medicine, New Brunswick 08901, USA.
P
P
Haluska
E H
EH
Rubin
D000952:Antigens, Polyomavirus Transforming / Q000378:metabolism*; D001816:Bloom Syndrome / Q000235:genetics; D004264:DNA Topoisomerases, Type I / Q000378:metabolism*; D006801:Humans; D009690:Nucleic Acid Conformation; D010750:Phosphoproteins / Q000378:metabolism; D011485:Protein Binding / Q000502:physiology; D016601:RNA-Binding Proteins / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D000097796:Nucleolin
D000952:Antigens, Polyomavirus Transforming; D004264:DNA Topoisomerases, Type I; D010750:Phosphoproteins; D016601:RNA-Binding Proteins; D011993:Recombinant Fusion Proteins; D000097796:Nucleolin