Purified Membrane-Containing Procapsids of Bacteriophage PRD1 Package the Viral Genome

Ziedaite, Gabija; Kivelä, Hanna M.; Bamford, Jaana K. H.; Bamford, Dennis H.

doi:10.1016/j.jmb.2008.12.068

Cited by 18 publications

(19 citation statements)

References 65 publications

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“…Therefore, in contrast to the tailed dsDNA phages, the PRD1 packaging enzyme is a structural protein and does not dissociate after the assembly is complete [17,212]. The rate of PRD1 packaging in vitro was calculated to be more than 340 bp/s [215], which is comparable with that of some dsDNA tailed phages (e.g., 350 bp/s for SPP1 [216]). Bacteriophage T4 can package with a rate of up to 2000 bp/s [217]), whereas dsRNA phages translocate RNA at a much slower rate of about 30 bp/s [218].…”

Section: Lipid Containing Phagesmentioning

confidence: 99%

Bacteriophage Assembly

Aksyuk

Rossmann

2011

Viruses

121

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Bacteriophages have been a model system to study assembly processes for over half a century. Formation of infectious phage particles involves specific protein-protein and protein-nucleic acid interactions, as well as large conformational changes of assembly precursors. The sequence and molecular mechanisms of phage assembly have been elucidated by a variety of methods. Differences and similarities of assembly processes in several different groups of bacteriophages are discussed in this review. The general principles of phage assembly are applicable to many macromolecular complexes.

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Section: Lipid Containing Phagesmentioning

confidence: 99%

Bacteriophage Assembly

Aksyuk

Rossmann

2011

Viruses

121

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“…4). The PRD1 ATPase mediates the genome packaging into the capsid (70,82); consequently, ORF 13 may also code for a packaging ATPase. The gene product of ORF 1 is similar to the replication initiation protein of Thermus sp.…”

Section: Lipid Composition Of P23-77 Differs From That Of the Hostmentioning

confidence: 99%

The Closest Relatives of Icosahedral Viruses of Thermophilic Bacteria Are among Viruses and Plasmids of the Halophilic Archaea

Jalasvuori

Jaatinen

Laurinavičius

et al. 2009

J Virol

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We have sequenced the genome and identified the structural proteins and lipids of the novel membranecontaining, icosahedral virus P23-77 of Thermus thermophilus. P23-77 has an ϳ17-kb circular double-stranded DNA genome, which was annotated to contain 37 putative genes. Virions were subjected to dissociation analysis, and five protein species were shown to associate with the internal viral membrane, while three were constituents of the protein capsid. Analysis of the bacteriophage genome revealed it to be evolutionarily related to another Thermus phage (IN93), archaeal Halobacterium plasmid (pHH205), a genetic element integrated into Haloarcula genome (designated here as IHP for integrated Haloarcula provirus), and the Haloarcula virus SH1. These genetic elements share two major capsid proteins and a putative packaging ATPase. The ATPase is similar with the ATPases found in the PRD1-type viruses, thus providing an evolutionary link to these viruses and furthering our knowledge on the origin of viruses.

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“…Current understanding is based primarily on what is known about the genome packaging ATPase P9 of bacteriophage PRD1 which stems from genetic studies and in vitro experiments using cell lysates. The ATPase itself has been intractable to structural characterization [34,35]. In PRD1-like viruses, with an ordered icosahedral capsid and an internal lipid membrane, small membrane proteins (P20 and P22 in PRD1) have been inferred to form a membrane pore at the packaging vertex, and they may function similarly to the connectors of head-tail phages [36].…”

Section: Introductionmentioning

confidence: 99%

“…In PRD1-like viruses, with an ordered icosahedral capsid and an internal lipid membrane, small membrane proteins (P20 and P22 in PRD1) have been inferred to form a membrane pore at the packaging vertex, and they may function similarly to the connectors of head-tail phages [36]. The packaging rate of the PRD1 machinery is 340 bp s −1 based on the time of the appearance of the first infectious particles [35], a value close to that described for phi29 gp16 and T4 gp17. We have recently gained some insight into the structure of a genome packaging ATPase from a PRD1-like virus, with the newly solved crystal structure of the STIV2 genome packaging ATPase, B204 [7] (discussed below).…”

Section: Introductionmentioning

confidence: 99%

Adenosine triphosphatases of thermophilic archaeal double-stranded DNA viruses

et al. 2014

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Adenosine triphosphatases (ATPases) of double-stranded (ds) DNA archaeal viruses are structurally related to the AAA+ hexameric helicases and translocases. These ATPases have been implicated in viral life cycle functions such as DNA entry into the host, and viral genome packaging into preformed procapsids. We summarize bioinformatical analyses of a wide range of archaeal ATPases, and review the biochemical and structural properties of those archaeal ATPases that have measurable ATPase activity. We discuss their potential roles in genome delivery into the host, virus assembly and genome packaging in comparison to hexameric helicases and packaging motors from bacteriophages.

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Purified Membrane-Containing Procapsids of Bacteriophage PRD1 Package the Viral Genome

Cited by 18 publications

References 65 publications

Bacteriophage Assembly

Bacteriophage Assembly

The Closest Relatives of Icosahedral Viruses of Thermophilic Bacteria Are among Viruses and Plasmids of the Halophilic Archaea

Adenosine triphosphatases of thermophilic archaeal double-stranded DNA viruses

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