|Entry||Database: EMDB / ID: EMD-4424|
|Title||Adenovirus major core protein condenses DNA in clusters and bundles, modulating genome release and capsid internal pressure.|
|Biological species||Ad5-VII-loxP (virus)|
|Method||single particle reconstruction / cryo EM / Resolution: 4.97 Å|
|Authors||Hernando-Perez M / San Martin M / Condezo GN / Hearing P|
|Funding support|| Spain, 1 items |
|Citation||Journal: Nucleic Acids Res. / Year: 2019|
Title: Adenovirus major core protein condenses DNA in clusters and bundles, modulating genome release and capsid internal pressure.
Authors: Natalia Martín-González / Mercedes Hernando-Pérez / Gabriela N Condezo / Marta Pérez-Illana / Antonio Šiber / David Reguera / Philomena Ostapchuk / Patrick Hearing / Carmen San Martín / Pedro J de Pablo /
Abstract: 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 ...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.
|Structure viewer||EM map: |
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|File||Download / File: emd_4424.map.gz / Format: CCP4 / Size: 1.6 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)|
|Projections & slices|
Images are generated by Spider.
|Voxel size||X=Y=Z: 1.37 Å|
|Symmetry||Space group: 1|
CCP4 map header:
|Entire||Name: Ad5-VII-loxP (virus) / Number of components: 1|
-Component #1: virus, Ad5-VII-loxP
|Virus||Name: Ad5-VII-loxP / Class: VIRION / Empty: No / Enveloped: No / Isolate: SEROTYPE|
|Mass||Theoretical: 150 MDa|
|Species||Species: Ad5-VII-loxP (virus)|
|Specimen||Specimen state: Particle / Method: cryo EM|
|Sample solution||Specimen conc.: 4.2 mg/mL / pH: 7.4|
|Vitrification||Instrument: LEICA EM CPC / Cryogen name: ETHANE|
-Electron microscopy imaging
Model: Talos Arctica / Image courtesy: FEI Company
|Imaging||Microscope: FEI TALOS ARCTICA|
|Electron gun||Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Electron dose: 50 e/Å2 / Illumination mode: FLOOD BEAM|
|Lens||Magnification: 73000.0 X (nominal), 73000.0 X (calibrated) / Cs: 2.7 mm / Imaging mode: BRIGHT FIELD / Defocus: 500.0 - 3000.0 nm|
|Specimen Holder||Model: FEI TITAN KRIOS AUTOGRID HOLDER|
|Camera||Detector: FEI FALCON II (4k x 4k)|
|Image acquisition||Number of digital images: 1640|
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