Structural modifications induced by the mtDBP-C protein in the replication origin of Xenopus laevis mitochondrial DNA

Mignotte, Bernard; Théveny, B; Révet, Bernard

doi:10.1016/0300-9084(90)90174-f

Cited by 8 publications

(3 citation statements)

References 27 publications

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“…It also allows induced DNA bending to be studied. This subject is treated in a related publication (Mignotte et al, 1990) concerning the influence of a mitochondrial protein on the conformation of the DNA helix.…”

Section: Discussionmentioning

confidence: 99%

Electron microscopy mapping of pBR322 DNA curvature. Comparison with theoretical models.

1990

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A map of local curvature of the pBR322 DNA has been established by electron microscopy analysis of linearized plasmid molecules. To determine their polarity these molecules are one end labelled with an avidin‐ferritin‐biotin complex and the images are digitized. Local curvature is calculated from two mathematical treatments of the DNA trajectory and expressed in term of a mean dinucleotide wedge angle. Eight regions of curvature are distinguished. The four main regions of curvature have a high content of phased AA runs. The experimental curvature map is compared to theoretical maps of curvature obtained from four available models for DNA curvature.

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Section: Discussionmentioning

confidence: 99%

Electron microscopy mapping of pBR322 DNA curvature. Comparison with theoretical models.

1990

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“…B R6vet and co-workers in our laboratory focus more precisely on the conformation of DNA molecules by the study of their local curvature, in relation to the sequence [43,72,101]. This procedure was applied to the analysis of DNA conformation modifications induced by protein interaction [34,60,61,88] (reviewed in [50]), or by intercalating drugs [5], even when DNA-binding drugs are not favorable for such a quantitative analysis [64]. Recently, we proposed an EM procedure of gene mapping based on single-stranded DNA-recA complex recognition of homologous sequences in double-stranded DNA [87].…”

Section: New Developmentsmentioning

confidence: 99%

Electron microscopy of macromolecules. The french contribution

DELAIN¹

1994

Biology of the Cell

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“…Electron microscopy analysis of the DNA-protein interaction shows that the mtDBP-C protein binds cooperatively (Mignotte et al, 1988) to the promoters and the replication origin and modifies the local conformation of the DNA by increasing its bending leading to condensed molecules (Mignotte et al, 1990). These properties could be implicated in the initiation of the mitochondria1 DNA replication, probably by allowing the binding of other proteins.…”

Section: Binding Of the Mtdbp-c Protein With The Regulatory Region Ofmentioning

confidence: 99%

Quantitative electron microscopic analysis of DNA‐protein interactions

Cam¹,

Théveny²,

Mignotte³

et al. 1991

J. Elec. Microsc. Tech.

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Electron microscopy offers a unique potentiality to visualize individual molecules. For the last 30 years it has been used to study the structure and the interactions of various biological macromolecules. The contribution of electron microscopy is important because of its capacity to demonstrate the existence of conformational structures such as kinks, bents, loops, etc., either on naked DNA, or on DNA associated with various proteins or ligands. Increasing interest was given to such observations when it was found that they provide a direct visualization of interacting molecules involved in DNA metabolism and gene regulation. Technical advances in the preparation of the specimens, their observation in the electron microscope, and the image processing by computers have allowed the shifting from qualitative to quantitative analysis, as illustrated by a few examples from our laboratory.

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Structural modifications induced by the mtDBP-C protein in the replication origin of Xenopus laevis mitochondrial DNA

Cited by 8 publications

References 27 publications

Electron microscopy mapping of pBR322 DNA curvature. Comparison with theoretical models.

Electron microscopy mapping of pBR322 DNA curvature. Comparison with theoretical models.

Electron microscopy of macromolecules. The french contribution

Quantitative electron microscopic analysis of DNA‐protein interactions

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