PubMed · 4697997
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M H Richmond. 1973. Plasmids in Staphylococcus aureus.. https://pubmed.ncbi.nlm.nih.gov/4697997/
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A method is offered for obtaining minimum energy configurations of DNA minicircles constrained by one or more DNA-binding proteins. The minicircles are modeled as elastic rods, while the presence of bound protein is implied by rigidly fixing portions of these chains. The configurations of the geometrically constrained circular rods are sampled stochastically and optimized according to a simple elastic energy model of nicked DNA. The shapes of the minimum energy structures identified after a simulated annealing process are analyzed in terms of relative protein orientation and writhing number. The procedure is applied to minicircles 500 base pairs in length, bound to two evenly spaced DNA-wrapping proteins. The presence of histone octamers is suggested by rigidly fixing the two protein-bound portions of each minicircle as small superhelices similar in dimension to nucleosomal DNA. The folded minimum energy forms of sample chains with different degrees of protein wrapping are noteworthy in themselves in that they offer a new resolution to the well-known minichromosome linking number paradox and point to future minicircle simulations of possible import.
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The purpose of this review is to present an account of our current understanding of the structure, organization and evolution of mitochondrial genomes, and to discuss the origin and evolution of mitochondria from the perspective recently provided by the extensive sequencing of various mitochondrial genomes. Mitochondrial-en-coded protein phylogenies are congruent with nuclear phylogenies and strongly support a monophyletic origin of mitochondria. The newly available data from red-algal mitochondrial genomes, in particular, show that the structural and functional diversity of mitochondrial genomes can be accounted for by paralogous evolution. We also discuss the influence of other constraints, such as uniparental inheritance, on the evolution of genome organization in mitochondria.