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Journal of Virology, November 2007, p. 12450-12457, Vol. 81, No. 22
0022-538X/07/$08.00+0 doi:10.1128/JVI.01470-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

and
Michael J. Imperiale*
Department of Microbiology and Immunology and Comprehensive Cancer Center, University of Michigan Medical School, 1500 E. Medical Center Dr., Ann Arbor, Michigan 48109
Received 5 July 2007/ Accepted 27 August 2007
Assembly of infectious adenovirus particles requires seven functionally redundant elements at the left end of the genome, termed A repeats, that direct packaging of the DNA. Previous studies revealed that the viral IVa2 protein alone interacts with specific sequences in the A repeats but that additional IVa2-containing complexes observed during infection require the viral L4 22-kDa protein. In this report, we purified a recombinant form of the 22-kDa protein to characterize its DNA binding properties. In electrophoretic mobility shift assay analyses, the 22-kDa protein alone did not interact with the A repeats but it did form complexes on them in the presence of the IVa2 protein. These complexes were identical to those seen in extracts from infected cells and had the same DNA sequence dependence. Furthermore, we provide data that the 22-kDa protein enhances binding of the IVa2 protein to the A repeats and that multiple binding sites in the packaging sequence augment this activity. These data support a cooperative role of the IVa2 and 22-kDa proteins in packaging and assembly.
Published ahead of print on 5 September 2007.
Present address: Department of Biological Sciences, Stanford University, Stanford, CA 94305-5020.
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