A role for the amino terminus of human topoisomerase I

Paul Haluska, Eric H. Rubin

Research output: Contribution to journalArticle

14 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)253-262
Number of pages10
JournalAdvances in Enzyme Regulation
Volume38
Issue number1
DOIs
StatePublished - Jul 1998
Externally publishedYes

Fingerprint

Type I DNA Topoisomerase
Bloom Syndrome
DNA Helicases
Yeast
Proteins
Yeasts
Antigens
DNA
In Vitro Techniques
nucleolin

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

A role for the amino terminus of human topoisomerase I. / Haluska, Paul; Rubin, Eric H.

In: Advances in Enzyme Regulation, Vol. 38, No. 1, 07.1998, p. 253-262.

Research output: Contribution to journalArticle

Haluska, Paul ; Rubin, Eric H. / A role for the amino terminus of human topoisomerase I. In: Advances in Enzyme Regulation. 1998 ; Vol. 38, No. 1. pp. 253-262.
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