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

• Published in: Journal of general virology 2003-12, Vol.84 (12), p.3423-3428
• Main Authors: Lee, Tim W. R, Blair, G. Eric, Matthews, David A
• Format: Article
• Language: English
• Subjects: Adenovirus; Adenoviruses, Human - chemistry; Adenoviruses, Human - physiology; Amino Acid Sequence; Cell Nucleolus - metabolism; Cell Nucleus - metabolism; Chromosomes, Human - metabolism; DNA Mutational Analysis; DNA, Viral - genetics; HeLa Cells; Humans; Molecular Sequence Data; Protein Binding; protein VII; Sequence Alignment; Viral Core Proteins - chemistry; Viral Core Proteins - genetics; Viral Core Proteins - metabolism; Virus Replication
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/vir.0.19546-0

1 School of Biochemistry and Molecular Biology, University of Leeds, Leeds LS2 9JT, UK 2 Department of Pathology and Microbiology, School of Medicine, University of Bristol, Bristol BS8 1TD, UK Correspondence Tim Lee timlee{at}doctors.org.uk During adenovirus infection, following capsid dissociation, core protein VII enters the host cell nucleus complexed with adenovirus DNA. In order to determine whether protein VII may have an active role in this nuclear import, regions of the preVII gene were amplified by PCR, and further oligonucleotide mutants were designed with site-directed mutation of codons for the basic amino acids arginine and lysine. Fragments were cloned into a mammalian expression plasmid to express the peptides as N-terminal fusions to enhanced green fluorescent protein. Results demonstrate that preVII protein contains both nuclear and nucleolar targeting sequences. 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.