Adenovirus type 2 terminal protein: purification and comparison of tryptic peptides with known adenovirus-coded proteins.
The protein covalently bound to the 5' termini of adenovirus type 2 DNA has been purified from virus labeled with [35S]methionine, using exclusion chromatography of disrupted virions to isolate the DNA-protein complex, which is then digested with DNase. The terminal protein isolated from mature virus is most effectively labeled if the cells are exposed to [35S]methionine during the "intermediate" period of 13 to 21 h postinfection, suggesting that the protein is synthesized during this interval. The tryptic peptides of the terminal protein were compared with those of several known adenovirus-coded proteins and found to be unrelated. In particular, the terminal protein is not related to the 38-50K early proteins encoded by the leftmost 4.4% of the adenovirus genome, one region essential for the transforming activity of the virus. Neither is it related to the 72K single-strand-specific DNA binding protein, the minor virion component IVa2, or the major capsid component hexon.
D000260:Adenoviruses, Human / Q000032:analysis* / Q000378:metabolism; D004279:DNA, Viral / Q000302:isolation & purification / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D010455:Peptides / Q000032:analysis; D014357:Trypsin; D014764:Viral Proteins / Q000032:analysis / Q000096:biosynthesis / Q000302:isolation & purification*
D004279:DNA, Viral; D010455:Peptides; D014764:Viral Proteins; D014357:Trypsin