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Nucleic Acids Research, 1979, Vol. 6, No. 6 2339-2353
© 1979

Articles

DNA-binding properties of the major core protein of adenovirus 2

Bruce C. Black and Melvin S. Center

Division of Biology, Kansas State University Manhattan, KS 66506, USA

Received December 27, 1978. The major adenovirus core protein (P·VII) binds to various species of duplex and single-stranded DNA molecules as a linear function of P·VII concentration. P·III progressively condenses 32S Ad2 DNA into rapidly sedimenting forms having an S value of around 2,280. P·VII does not coat DNA like cytochrome C, instead DNA-protein beads are visualized in the electron microscope at low protein concentration. These beads appear to interact forming larger structures and at high P·VII concentrations the DNA molecule becomes highly compacted. Analysis of DNA fragments formed after digestion of P·VII-DNA complexes and isolated cores with micrococcal nuclease suggest that the organization of the DNA in the two structures is essentially identical. The initial P·VII and DNA interaction is sensitive to both ionic and hydrophobic environments, whereas the in vitro DNA-P·VII complexes are extremely stable and are not disrupted in the presence of 3 M NaCl, 1% sarcosyl or 5% deoxycholate. Properties of these in vitro DNA-protein VII complexes share striking simi larities to isolated viral core particles.


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