Journal
NUCLEIC ACIDS RESEARCH
Volume 47, Issue 17, Pages 9231-9242Publisher
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkz687
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Funding
- Spanish Ministry of Economy and Competitivity [FIS201789549-R, MDM-2014-0377, FIS2017-90701-REDT]
- Human Frontiers Science Program [HFSPO RGP0012/2018]
- Spanish State Research Agency [BFU2016-74868-P]
- European Regional Development Fund [BFU2016-74868-P]
- Spanish Ministry of Economy, Industry and Competitivity [BIO2015-68990-REDT]
- MINECO/FEDER, UE [FIS2015-67837-P]
- National Institutes of Health [CA122677, AI102577]
- Juan de la Cierva postdoctoral contract - Spanish Ministry of Economy and Competitivity
- La Caixa Foundation
- Secretar'ia de Estado de Investigacion, Desarrollo e Innovacion [FIS2017-89549-R]
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Some viruses package dsDNA together with large amounts of positively charged proteins, thought to help condense the genome inside the capsid with no evidence. Further, this role is not clear because these viruses have typically lower packing fractions than viruses encapsidating naked dsDNA. In addition, it has recently been shown that the major adenovirus condensing protein (polypeptide VII) is dispensable for genome encapsidation. Here, we study the morphology and mechanics of adenovirus particles with (Ad5-wt) and without (Ad5-VII-) protein VII. Ad5-VII- particles are stiffer than Ad5-wt, but DNA-counterions revert this difference, indicating that VII screens repulsive DNA-DNA interactions. Consequently, its absence results in increased internal pressure. The core is slightly more ordered in the absence of VII and diffuses faster out of Ad5-VII-than Ad5-wt fractured particles. In Ad5-wt unpacked cores, dsDNA associates in bundles interspersed with VII-DNA clusters. These results indicate that protein VII condenses the adenovirus genome by combining direct clustering and promotion of bridging by other core proteins. This condensation modulates the virion internal pressure and DNA release from disrupted particles, which could be crucial to keep the genome protected inside the semi-disrupted capsid while traveling to the nuclear pore.
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