The structure of nucleoprotein cores released from adenovirions

Abstract

The morphology, protein composition and DNA organization of nucleoprotein core complexes isolated from type 5 adenovirions have been examined by electron microscopy and biochemical techniques. The morphology of such core structures is in some ways strikingly similar to that exhibited by cellular chromatin. 'Native' core preparations contain compact and less highly-folded forms: the latter appear as thick fibres, 150-300A in diameter. Upon exposure to 0.4M NaCl, adenovirus cores undergo a transition to a beaded string form, reminiscent of nucleosomes. Of the three arginine-rich proteins, polypeptides V, VII and mu present in 'native' cores, only polypeptide VII remains associated with viral DNA in the presence of 0.4M NaCl. We therefore conclude that the nucleosome-like beads are constructed solely of polypeptide VII. The results of micrococcal nuclease digestion experiments suggest that polypeptide VII is sufficient to protect some 100-300bp of adenoviral DNA.

Precursor of human adenovirus core polypeptide Mu targets the nucleolus and modulates the expression of E2 proteins

“…This viral DNA is covalently linked to viral terminal protein and non-covalently bound to the viral core proteins Mu, V and VII (reviewed by Shenk, 2001). Protein V, found only in mastadenoviruses (Davison et al, 2003), is believed to form a link between the viral DNA-core protein complex and the viral capsid (Matthews & Russell, 1998b), while proteins VII and Mu are tightly associated with the viral DNA (Chatterjee et al, 1985;Vayda et al, 1983).…”

Adenovirus core protein VII contains distinct sequences that mediate targeting to the nucleus and nucleolus, and colocalization with human chromosomes

“…Such signals may be important in the delivery of adenovirus DNA to the host cell nucleus during adenovirus infection. Furthermore, the data suggest that protein VII may bind to human chromosomes by means of two distinct domains, one sharing homology with the N-terminal regulatory tail of histone H3.Enclosed by approximately 12 capsid proteins the human adenovirus genome, comprising approximately 36 kb of linear double-stranded DNA, is non-covalently bound to the viral core proteins Mu, V, and VII (Vayda et al, 1983). Proteins VII and Mu are tightly associated with the viral DNA (Vayda et al, 1983;Chatterjee et al, 1985), whilst protein V may form a link between the viral DNA-core protein complex and the viral capsid (Matthews & Russell, 1998).…”

“…Enclosed by approximately 12 capsid proteins the human adenovirus genome, comprising approximately 36 kb of linear double-stranded DNA, is non-covalently bound to the viral core proteins Mu, V, and VII (Vayda et al, 1983). Proteins VII and Mu are tightly associated with the viral DNA (Vayda et al, 1983;Chatterjee et al, 1985), whilst protein V may form a link between the viral DNA-core protein complex and the viral capsid (Matthews & Russell, 1998).…”

“…Proteins VII and Mu are tightly associated with the viral DNA (Vayda et al, 1983;Chatterjee et al, 1985), whilst protein V may form a link between the viral DNA-core protein complex and the viral capsid (Matthews & Russell, 1998).…”

Fluorescence Tracking of Genome Release during Mechanical Unpacking of Single Viruses

“…The adenovirus genome is a mini-chromosome composed of a 35 kbp long dsDNA molecule and about 25 MDa of condensing proteins. [37][38][39][40][41] The exact architecture of this DNA-protein core is unknown. Adenoviruses assemble in the nucleus of the infected cell, and require a maturation step to become infectious.…”