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. 1986 Aug 11;14(15):5969–5980. doi: 10.1093/nar/14.15.5969

Characterization of a Xenopus laevis mitochondrial protein with a high affinity for supercoiled DNA.

B Mignotte, M Barat
PMCID: PMC311615  PMID: 3748802

Abstract

A DNA binding protein of 31 Kd -mtDBPC- has been isolated from X. laevis oocyte mitochondria. It is present in large amounts in the organelle and does not show any enzymatic activity. Its binding to the superhelical form of a DNA is higher than for any other form, or for RNA. No sequence specificity could be found for any mtDNA fragments tested, including both origins of replication. It is able to introduce superhelical turns into relaxed circular DNA in the presence of a topoisomerase I activity. It could be a component of the mitochondrial nucleoids.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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