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Virus DNA translocation: progress towards a first ascent of mount pretty difficult.

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Affiliations

  • 1. Department of Microbiology, Roy J. and Lucille A. Carver College of Medicine, University of Iowa, Iowa City, IA 52242, USA.
      Authors
    • Maluf NK 1
    (1 author)

Molecular Microbiology, 01 Jul 2006, 61(1):1-4
https://doi.org/10.1111/j.1365-2958.2006.05214.x PMID: 16824089 

This is a comment on "Portal fusion protein constraints on function in DNA packaging of bacteriophage T4." Mol Microbiol. 2006 Jul;61(1):16-32.

Abstract 

Virion DNA molecules of large dsDNA viruses are highly condensed. To pack the DNA, an ATP hydrolysis-powered motor translocates the DNA into a preformed empty protein shell, the prohead. The icosahedral prohead has a special fivefold vertex, the portal vertex, where the translocation machinery acts. The portal vertex contains the portal protein, a gear-shaped dodecamer of radially disposed subunits with a central channel for DNA entry. The symmetry mismatch between the fivefold symmetry of the shell vertex and the 12-fold symmetry of the portal protein has prompted DNA packaging models in which ATP-driven portal protein rotation drives DNA translocation. In this issue of Molecular Microbiology, Baumann and colleagues test portal rotation models using bacteriophage T4. A fusion between the gp20 portal protein and the HOC external shell decoration protein is used to create a block to portal rotation. Finding that DNA packaging is unimpeded in proheads containing the fusion argues that portal rotation is not crucial to DNA translocation. The paper is a landmark for describing direct testing of the mechanism of DNA translocation.

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Read article at publisher's site: https://doi.org/10.1111/j.1365-2958.2006.05214.x

Read article for free, from open access legal sources, via Unpaywall: https://onlinelibrary.wiley.com/doi/pdfdirect/10.1111/j.1365-2958.2006.05214.xUnpaywall

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