On the Mechanism of Adenovirus DNA Replication

Tamanoi, Fuyuhiko

doi:10.1007/978-1-4613-2293-1_3

Cited by 6 publications

(3 citation statements)

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“…The replication of the PRD1 genome follows the basic principles of a protein-primed mechanism (reviewed in 13). This replication mechanism has been extensively described in both adenovirus (14) and Bacillus subtilis phage 429, the latter being the best understood protein-primed replication system of prokaryotic origin (13,15). Previous work on the replication of bacteriophage PRD1 DNA led to the purification of both TP and phage DNA polymerase (16,17), as well as to the isolation of the phage genome (18), and resulted in a minimal in vitro replication system.…”

Section: Introductionmentioning

confidence: 99%

In Vitroreplication of bacteriophage PRD1 DNA. Characterization of the protein-primed initiation site

et al. 1993

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Bacteriophage PRD1 replicates its DNA by means of a protein-primed replication mechanism. Using single-stranded oligonucleotide templates carrying the sequence corresponding to the 25 first bases of the 3' end of PRD1 DNA, and Mg2+ as the activating metal ion of the phage DNA polymerase, we show that the fourth base from the 3' end of the template directs, by base complementarity, the dNMP to be linked to the phage terminal protein (TP) in the initiation reaction. This result suggests that phage PRD1 maintains its 3' end DNA sequences via a sliding-back mechanism. The single-stranded DNA templates could not be replicated by the PRD1 DNA polymerase, much in contrast to the natural TP-DNA. Nevertheless, the analysis of the transition products obtained with TP-DNA and origin-containing oligonucleotides suggests that sliding-back occurs stepwise, the fourth base being the directing position during the entire process.

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Section: Introductionmentioning

confidence: 99%

In Vitroreplication of bacteriophage PRD1 DNA. Characterization of the protein-primed initiation site

et al. 1993

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“…The dsDNA genome, which is packaged within the membrane vesicle, is a linear molecule of approximately 14700 base pairs (McGraw et al, 1983). As in the cases of adenovirus (Tamanoi, 1986) and bacteriophage 29 (Salas, 1988), a protein which primes DNA replication is covalently linked to the 5' terminus of each strand of PRD1 DNA (Bamford & Mindich, 1984).…”

mentioning

confidence: 99%

Structural study of the lipid-containing bacteriophage PRD1 and its capsid and DNA components by laser Raman spectroscopy

Bamford¹,

Bamford²,

Towse³

et al. 1990

Biochemistry

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The Raman spectrum of a virus contains the structural signature of each of its molecular components (Thomas, 1987). We report the first Raman spectrum obtained from an intact, lipid-containing virus--the icosahedral bacteriophage PRD1--and show that this spectrum contains characteristic structure markers for the major capsid protein, the packaged double-stranded DNA genome, and the viral membrane which resides between the capsid and DNA. We find that the packaged genome of PRD1 exhibits Raman markers typical of the B-DNA secondary structure. Comparison of the Raman spectrum of the packaged DNA with that of protein-free DNA extracted from the virion shows further that the B-form secondary structure is not significantly perturbed by packaging in the virion. The Raman signature of the PRD1 membrane, monitored within the virion at 4 degrees C, is that of a phospholipid liquid-crystalline phase. The PRD1 capsid, which comprises several hundred copies of the major coat protein P3 (product of viral gene III) and a few copies of minor proteins, incorporates P3 capsomers predominantly in the beta-sheet conformation. The beta-sheet structure of P3 is maintained in the fully assembled PRD1 virion, as well as in the empty capsid. The present results demonstrate the feasibility of obtaining structural information from the three different classes of biomolecules--nucleic acid, protein, and lipid--which constitute a membrane-lined virus particle. Our results also demonstrate that the coat protein and double-stranded DNA components of a lipid-containing bacteriophage share many structural features in common with bacteriophage lacking a lipid membrane.

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“…Adenovirus has a linear double-stranded DNA genome of about 35 kbp, with inverted terminal repeats (ITRs) and a covalently linked terminal protein (TP) attached to the 5' termini (Rekosh et al, 1977). The mechanism of replication has been analysed extensively in vivo and in vitro and a number of reviews have been published which provide detailed information on earlier studies in this area Friefeld et al, 1984;Tamanoi, 1986).…”

Section: Adenovirus Dna Replicationmentioning

confidence: 99%