title: The Xenopus laevis mitochondrial protein mtDBP-C cooperatively folds the DNA in vitro.
abstract: The binding of the Xenopus laevis mitochondrial protein mtDBP-C to DNA was studied by equilibrium density banding, agarose gel electrophoresis and electron microscopy. The results obtained show that the mtDBP-C binds cooperatively to DNA irrespective of whether the DNA is supercoiled, relaxed or linear and it induces the formation of superhelical turns locally leading to the formation of a highly folded structure. It appears that this protein could be involved in the compaction of DNA in the mitochondrial nucleoid.
authors.affiliation: Laboratoire de Biologie Générale, Université de Paris-Sud, Orsay, France.
authors.forename: B
authors.initials: B
authors.lastname: Mignotte
authors.forename: E
authors.initials: E
authors.lastname: Delain
authors.forename: D
authors.initials: D
authors.lastname: Rickwood
authors.forename: M
authors.initials: M
authors.lastname: Barat-Gueride
mesh_terms: D000818:Animals; D004272:DNA, Mitochondrial / Q000378:metabolism* / Q000648:ultrastructure; D004278:DNA, Superhelical / Q000378:metabolism / Q000648:ultrastructure; D004268:DNA-Binding Proteins / Q000502:physiology*; D003852:Deoxyribonucleoproteins / Q000648:ultrastructure; D008854:Microscopy, Electron; D012965:Sodium Chloride / Q000494:pharmacology; D014982:Xenopus laevis
chemical_list: D004272:DNA, Mitochondrial; D004278:DNA, Superhelical; D004268:DNA-Binding Proteins; D003852:Deoxyribonucleoproteins; D012965:Sodium Chloride