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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. Key words: darkfield electron microscopy/DNA-binding protein/DNA supercoiling/mitochondria of superhelical turns into relaxed circular DNA in the presence of topoisomerase I (Mignotte and Barat, 1986). The work presented here has been undertaken to characterize further the binding of mtDBP-C to DNA. Results Density of the mtDBP-C supercoiled DNA complexes in caesium chlorde The binding of mtDBP-C to supercoiled DNA was studied by equilibrium density banding experiments. The complexes formed in the presence of [3H]pXlmH5 DNA (4 ,ug; 1.70 g/cm3 1.56 gcm3
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https://hal.uvsq.fr/hal-03038243
Contributor : Bernard Mignotte Connect in order to contact the contributor
Submitted on : Friday, December 18, 2020 - 4:44:34 PM
Last modification on : Monday, October 25, 2021 - 2:26:33 PM

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  • HAL Id : hal-03038243, version 1

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Bernard Mignotte, Etienne Delain2, David Rickwood3, Monique Barat-Gueride1. The Xenopus laevis mitochondrial protein mtDBP-C cooperatively folds the DNA in vitro. EMBO Journal, EMBO Press, 1988. ⟨hal-03038243⟩

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