TY - JOUR
T1 - Comparison of the interactions of the adenovinis type 2 major core protein and its precursor with DNA
AU - Chatterjee, Pradeep K.
AU - Yang, U. C.
AU - Flint, S. J.
N1 - Funding Information:
ACKKOWLEDGEHEMTS This work was supported by a grant (#HP 464G) froa the Amerioan Cancer Society. He thank Tom Rooney for helpful disousslons and Margie Toung and Seema ChatterJee for excellent technical assistance.
PY - 1986/3/11
Y1 - 1986/3/11
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0023056519&partnerID=8YFLogxK
U2 - 10.1093/nar/14.6.2721
DO - 10.1093/nar/14.6.2721
M3 - Article
C2 - 3960731
AN - SCOPUS:0023056519
SN - 0305-1048
VL - 14
SP - 2721
EP - 2735
JO - Nucleic acids research
JF - Nucleic acids research
IS - 6
ER -