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.