Intranuclear location of the adenovirus type 5 E1B 55-kilodalton protein.
The intracellular location of the adenovirus type 5 E1B 55-kilodalton (kDa) protein, particularly the question of whether it is associated with nuclear pore complexes, was examined. Fractionation of adenovirus type 5-infected HeLa cell nuclei by an established procedure (N. Dwyer and G. Blobel, J. Cell. Biol. 70:581-591, 1976) yielded one population of E1B 55-kDa protein molecules released by digestion of nuclei with RNase A and a second population recovered in the pore complex-lamina fraction. Free and E1B 55-kDa protein-bound forms of the E4 34-kDa protein (P. Sarnow, C. A. Sullivan, and A. J. Levine, Virology 120:387-394, 1982) were largely recovered in the pore complex-lamina fraction. Nevertheless, the association of E1B 55-kDa protein molecules with this nuclear envelope fraction did not depend on interaction of the E1B 55-kDa protein with the E4 34-kDa protein. Comparison of the immunofluorescence patterns observed with antibodies recognizing the E1B 55-kDa protein or cellular pore complex proteins and of the behavior of these viral and cellular proteins during in situ fractionation suggests that the E1B 55-kDa protein does not become intimately or stably associated with pore complexes in adenovirus-infected cells.
Smiley
J K
JK
Department of Biology, Princeton University, New Jersey 08544.
Young
M A
MA
Flint
S J
SJ
D017456:Adenovirus Early Proteins; D000260:Adenoviruses, Human / Q000235:genetics*; D002467:Cell Nucleus / Q000032:analysis / Q000378:metabolism / Q000648:ultrastructure; D004591:Electrophoresis, Polyacrylamide Gel; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D008970:Molecular Weight; D009856:Oncogene Proteins, Viral / Q000032:analysis* / Q000235:genetics
D017456:Adenovirus Early Proteins; D009856:Oncogene Proteins, Viral