title: Human DNA topoisomerase IB: structure and functions.
abstract: Human DNA Topoisomerase I is a 765aa monomeric enzyme composed of four domains: the N-terminal domain, highly charged and responsible for several protein-protein interactions, the core domain that embraces the DNA during catalysis, the highly charged linker domain and the C-teminal domain containing the active site. The enzyme promotes the relaxation of supercoiled DNA by nicking and rejoining one of the strands of the DNA. Its activity is critical for many biological processes including DNA replication, transcription, and recombination. The aim of this review is to analyze the enzyme activity in terms of structure-function relationship.
authors.affiliation: Department of Biology, University of Padova, Padova, Italy.
authors.forename: Erica
authors.initials: E
authors.lastname: Cretaio
authors.forename: Luca
authors.initials: L
authors.lastname: Pattarello
authors.forename: Yari
authors.initials: Y
authors.lastname: Fontebasso
authors.forename: Piero
authors.initials: P
authors.lastname: Benedetti
authors.forename: Carmen
authors.initials: C
authors.lastname: Losasso
mesh_terms: D002384:Catalysis; D004261:DNA Replication / Q000502:physiology*; D004264:DNA Topoisomerases, Type I / Q000737:chemistry / Q000378:metabolism*; D004278:DNA, Superhelical / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D017434:Protein Structure, Tertiary / Q000502:physiology; D011995:Recombination, Genetic / Q000502:physiology*; D013329:Structure-Activity Relationship; D014158:Transcription, Genetic / Q000502:physiology*
chemical_list: D004278:DNA, Superhelical; D004264:DNA Topoisomerases, Type I