The Xenopus laevis mitochondrial protein mtDBP-C cooperatively folds the DNA in vitro.
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.
Mignotte
B
B
Laboratoire de Biologie Générale, Université de Paris-Sud, Orsay, France.
Delain
E
E
Rickwood
D
D
Barat-Gueride
M
M
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
D004272:DNA, Mitochondrial; D004278:DNA, Superhelical; D004268:DNA-Binding Proteins; D003852:Deoxyribonucleoproteins; D012965:Sodium Chloride