Smart, J. E., Stillman, B. W. (1982) Adenovirus terminal protein precursor. Partial amino acid sequence and the site of covalent linkage to virus DNA. Journal of Biological Chemistry, 257 (22). pp. 13499-13506. ISSN 00219258 (ISSN)
Abstract
The adenovirus terminal protein precursor functions as a primer for the initiation of virus DNA replication by covalently binding the first nucleotide in the DNA chain. It remains covalently attached to the 5'-ends of the virus DNA and is cleaved to the terminal protein during virion maturation. The gene encoding the terminal protein precursor maps within a 7-kilobase region of the virus genome, which specifies multiple mRNA and protein species. We have determined the location, within this region, of the coding sequences for the terminal protein precursor by aligning partial amino acid sequence to the amino acid sequence predicted from the DNA sequence. The open translational reading frame between coordinates 23.4 and 28.9 on the genome contains the majority of the coding sequences for the precursor protein. The virion terminal protein derives from COOH terminus of the precursor protein. Using this information, the site within the protein of covalent attachment to the DNA has been determined. This site also corresponds to that which covalently binds dCMP, the first nucleotide in nascent DNA synthesized in vitro. The coding region for terminal protein precursor does not overlap the region to which the N-group of adenovirus mutants has been mapped. We suggest that these mutants define a protein, other than terminal protein, which also functions in the initiation of virus DNA replication.
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