The Structure of an Infectious P22 Virion Shows the Signal for Headful DNA Packaging

Lander, Gabriel C.; Tang, Liang; Casjens, Sherwood; Gilcrease, Eddie B.; Prevelige, Peter E.; Poliakov, Anton; Potter, Clinton S.; Carragher, Bridget; Johnson, John E.

doi:10.1126/science.1127981

Cited by 289 publications

(413 citation statements)

References 19 publications

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“…At the same time, DNA near the center of the capsid is highly disordered even though the global organization is coaxially-spooled. This is consistent with the DNA structures observed by cryo-EM in ε15 and P22 Lander et al, 2006). Besides this, neither of the two packaging motifs considered so far (Figures 2a and 2b) exhibit geometrically idealized conformations such those of Arsuaga et al (Arsuaga et al, 2002).…”

Section: Isometric Capsids With a Core: Simulation Of ε15supporting

confidence: 78%

“…2D studies on the icosahedral phage T7 with a large protein core revealed that DNA forms a set of rings around the protein core and supported the coaxial spooling model (Cerritelli et al, 1997). Similar conformations were revealed by higher-resolution 3D reconstructions on phages ε15 and P22 Lander et al, 2006), which are both isomorphous to T7 (Agirrezabala et al, 2005). 3D density reconstruction of prolate ϕ29 showed a set of concentric ellipsoidal shells of DNA density (Tao et al, 1998;Xiang et al, 2006) but failed to resolve individual DNA strands.…”

Section: Introductionmentioning

confidence: 68%

“…In both models (those that include electrostatics and those that don't), DNA ordering is more pronounced at the outer layers than in the interior, where the bending stresses are higher and there is more conformational variability. Although the DNA is significantly ordered overall, the conformations are far from the ideal close-packed conformations that one might infer from the concentric rings of density seen in cryo-EM studies, both two-dimensional projections (Cerritelli et al, 1997) and three-dimensional reconstructions Lander et al, 2006Xiang et al, 2006).…”

Section: Discussionmentioning

confidence: 99%

“…ε15 , T7 (Agirrezabala et al, 2005) and P22 Lander et al, 2006), that contain a large protein portal complex located at one of the capsid's vertices. Inspired by these results we have simulated the packaging of dsDNA into a detailed model for ε15 .…”

Section: Isometric Capsids With a Core: Simulation Of ε15mentioning

confidence: 99%

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The conformation of double-stranded DNA inside bacteriophages depends on capsid size and shape

Petrov

Boz

Harvey

2007

Journal of Structural Biology

108

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The packaging of double-stranded DNA into bacteriophages leads to the arrangement of the genetic material into highly-packed and ordered structures. Although modern experimental techniques reveal the most probable location of DNA inside viral capsids, the individual conformations of DNA are yet to be determined. In the current study we present the results of molecular dynamics simulations of the DNA packaging into several bacteriophages performed within the framework of a coarse-grained model. The final DNA conformations depend on the size and shape of the capsid, as well as the size of the protein portal, if any. In particular, isometric capsids with small or absent portals tend to form concentric spools, whereas the presence of a large portal favors coaxial spooling; slightly and highly elongated capsids result in folded and twisted toroidal conformations, respectively. The results of the simulations also suggest that the predominant factor in defining the global DNA arrangement inside bacteriophages is the minimization of the bending stress upon packaging.

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Section: Isometric Capsids With a Core: Simulation Of ε15supporting

confidence: 78%

Section: Introductionmentioning

confidence: 68%

Section: Discussionmentioning

confidence: 99%

Section: Isometric Capsids With a Core: Simulation Of ε15mentioning

confidence: 99%

See 2 more Smart Citations

The conformation of double-stranded DNA inside bacteriophages depends on capsid size and shape

Petrov

Boz

Harvey

2007

Journal of Structural Biology

108

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“…These studies combine data from thousands of particles to produce three-dimensional images of the capsid and genomic DNA, allowing the visualization of several layers of DNA loops within the capsid. [11][12][13] Models of Tightly-Packed Viral DNA…”

Section: Dna Virusesmentioning

confidence: 99%

Biological consequences of tightly bent DNA: The other life of a macromolecular celebrity

et al. 2006

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The mechanical properties of DNA play a critical role in many biological functions. For example, DNA packing in viruses involves confining the viral genome in a volume (the viral capsid) with dimensions that are comparable to the DNA persistence length. Similarly, eukaryotic DNA is packed in DNA-protein complexes (nucleosomes) in which DNA is tightly bent around protein spools. DNA is also tightly bent by many proteins that regulate transcription, resulting in a variation in gene expression that is amenable to quantitative analysis. In these cases, DNA loops are formed with lengths that are comparable to or smaller than the DNA persistence length. The aim of this review is to describe the physical forces associated with tightly bent DNA in all of these settings and to explore the biological consequences of such bending, as increasingly accessible by single-molecule techniques.

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Insights into virus capsid assembly from non‐covalent mass spectrometry

Morton

Stockley

Stonehouse

et al. 2008

Mass Spectrometry Reviews

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The assembly of viral proteins into a range of macromolecular complexes of strictly defined architecture is one of Nature's wonders. Unraveling the details of these complex structures and the associated self-assembly pathways that lead to their efficient and precise construction will play an important role in the development of anti-viral therapeutics. It will also be important in bio-nanotechnology where there is a plethora of applications for such well-defined macromolecular complexes, including cell-specific drug delivery and as substrates for the formation of novel materials with unique electrical and magnetic properties. Mass spectrometry has the ability not only to measure masses accurately but also to provide vital details regarding the composition and stoichiometry of intact, non-covalently bound macromolecular complexes under near-physiological conditions. It is thus ideal for exploring the assembly and function of viruses. Over the past decade or so, significant advances have been made in this field, and these advances are summarized in this review, which covers the literature up to the end of 2007.

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The Structure of an Infectious P22 Virion Shows the Signal for Headful DNA Packaging

Cited by 289 publications

References 19 publications

The conformation of double-stranded DNA inside bacteriophages depends on capsid size and shape

The conformation of double-stranded DNA inside bacteriophages depends on capsid size and shape

Biological consequences of tightly bent DNA: The other life of a macromolecular celebrity

Insights into virus capsid assembly from non‐covalent mass spectrometry

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