The interactions of the major core protein of adenovirus type 2 (Ad2) protein VII, and its precursor, protein pre-VII, with viral DHA, were studied using UV light induoed crossllnklng of 32P-labelled ollgonuoleotldes to the proteins. Proteolytio fragments of these two proteins that oontaln DNA-bindlng donalns were Identified by virtue of their oovalently attaohed, alkali-resistant 32P-radioaotivity. The overall effioienoy of orossllnking of protein pre-VII to DHA, in H2ts1 virions assembled at 39°C, was comparable to that of the orosslinklng of protein Til to DHA in Ad2 virions. However, a protease T8 fragment comprising the H-terminal half of protein pre-VII orosslinked to DHA at least ten tines Bore efficiently than the corresponding B-termlnal fragnent of protein Til, whlob is truncated by the reaoval of 23 amino adds fron the H-temlnus of protein pre-VII during virion saturation.
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