Processing of Adenovirus 2-Induced Proteins

C. W. Anderson; P. R. Baum; R. F. Gesteland

doi:10.1128/jvi.12.2.241-252.1973

J Virol. 1973 Aug; 12(2): 241–252.

doi: 10.1128/jvi.12.2.241-252.1973

PMCID: PMC356618

PMID: 4747985

Processing of Adenovirus 2-Induced Proteins

C. W. Anderson, P. R. Baum, and R. F. Gesteland

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Abstract

Analysis of ³⁵S-methionine-labeled extracts of adenovirus 2-infected KB cells revealed 22 virus-induced polypeptide components. Most proteins of the virion were easily detected in extracts of whole cells labeled for short periods between 15 and 30 h after infection; however, several virion components were conspicuously absent. Radioactivity appeared in two of these virion components during a chase in nonradioactive medium, and this appearance was paralleled by a decrease in the radioactivity associated with two nonvirion adenovirus-induced proteins, results which imply precursor-product relationships for these components. Comparison of one of the chasable adenovirus-induced components (designated P-VII; mass of 20,000 daltons) and the major core protein (VII; mass of 18,500 daltons) of the virion showed that they have four common methionine-containing tryptic peptides; P-VII has an additional methionine residue which is not found in the major core protein. We propose that at least two of the adenovirus 2 virion components are derived by the cleavage of higher molecular weight precursor polypeptides.

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Selected References

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