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EMBO J
1988 Dec 01;712:3873-9. doi: 10.1002/j.1460-2075.1988.tb03273.x.
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The Xenopus laevis mitochondrial protein mtDBP-C cooperatively folds the DNA in vitro.
Mignotte B
,
Delain E
,
Rickwood D
,
Barat-Gueride M
.
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.
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