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Coexistence of coil and globule domains within a single confined DNA chain

The highly charged DNA chain may be either in an extended conformation, the coil, or condensed into a highly dense and ordered structure, the toroid. The transition, also called collapse of the chain, can be triggered in different ways, for example by changing the ionic conditions of the solution. W...

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Autores principales: Sung, Baeckkyoung, Leforestier, Amélie, Livolant, Françoise
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2016
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4756835/
https://www.ncbi.nlm.nih.gov/pubmed/26704970
http://dx.doi.org/10.1093/nar/gkv1494
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author Sung, Baeckkyoung
Leforestier, Amélie
Livolant, Françoise
author_facet Sung, Baeckkyoung
Leforestier, Amélie
Livolant, Françoise
author_sort Sung, Baeckkyoung
collection PubMed
description The highly charged DNA chain may be either in an extended conformation, the coil, or condensed into a highly dense and ordered structure, the toroid. The transition, also called collapse of the chain, can be triggered in different ways, for example by changing the ionic conditions of the solution. We observe individual DNA molecules one by one, kept separated and confined inside a protein shell (the envelope of a bacterial virus, 80 nm in diameter). For subcritical concentrations of spermine (4+), part of the DNA is condensed and organized in a toroid and the other part of the chain remains uncondensed around. Two states coexist along the same DNA chain. These ‘hairy’ globules are imaged by cryo-electron microscopy. We describe the global conformation of the chain and the local ordering of DNA segments inside the toroid.
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spelling pubmed-47568352016-02-18 Coexistence of coil and globule domains within a single confined DNA chain Sung, Baeckkyoung Leforestier, Amélie Livolant, Françoise Nucleic Acids Res Structural Biology The highly charged DNA chain may be either in an extended conformation, the coil, or condensed into a highly dense and ordered structure, the toroid. The transition, also called collapse of the chain, can be triggered in different ways, for example by changing the ionic conditions of the solution. We observe individual DNA molecules one by one, kept separated and confined inside a protein shell (the envelope of a bacterial virus, 80 nm in diameter). For subcritical concentrations of spermine (4+), part of the DNA is condensed and organized in a toroid and the other part of the chain remains uncondensed around. Two states coexist along the same DNA chain. These ‘hairy’ globules are imaged by cryo-electron microscopy. We describe the global conformation of the chain and the local ordering of DNA segments inside the toroid. Oxford University Press 2016-02-18 2015-12-23 /pmc/articles/PMC4756835/ /pubmed/26704970 http://dx.doi.org/10.1093/nar/gkv1494 Text en © The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. http://creativecommons.org/licenses/by-nc/4.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com
spellingShingle Structural Biology
Sung, Baeckkyoung
Leforestier, Amélie
Livolant, Françoise
Coexistence of coil and globule domains within a single confined DNA chain
title Coexistence of coil and globule domains within a single confined DNA chain
title_full Coexistence of coil and globule domains within a single confined DNA chain
title_fullStr Coexistence of coil and globule domains within a single confined DNA chain
title_full_unstemmed Coexistence of coil and globule domains within a single confined DNA chain
title_short Coexistence of coil and globule domains within a single confined DNA chain
title_sort coexistence of coil and globule domains within a single confined dna chain
topic Structural Biology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4756835/
https://www.ncbi.nlm.nih.gov/pubmed/26704970
http://dx.doi.org/10.1093/nar/gkv1494
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