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Biphasic Packing of DNA and Internal Proteins in Bacteriophage T4 Heads Revealed by Bubblegram Imaging.
Viruses
November 2020
Laboratory of Structural Biology Research, National Institute of Arthritis Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, MD 20892-8025, USA.
Article Synopsis
- Tailed bacteriophages and herpesviruses contain condensed DNA and significant amounts of internal proteins that aid in various functions like scaffolding and delivery.
- The study used bubblegram imaging to analyze the distribution of internal proteins in the T4 bacteriophage, discovering that bubbles indicate protein presence rather than DNA.
- The T4 head has a bubble-free zone beneath the capsid shell, likely filled with ordered DNA layers, while internal proteins create bubbles in a disordered arrangement within the remaining space.
A Cut above the Rest: Characterization of the Assembly of a Large Viral Icosahedral Capsid.
Viruses
July 2020
Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, Rochester, NY 14623, USA.
The head of virus SPN3US is composed of ~50 different proteins and is unusual because within its packaged genome there is a mass (>40 MDa) of ejection or E proteins that enter the cell. The assembly mechanisms of this complex structure are poorly understood. Previous studies showed that eight proteins in the mature SPN3US head had been cleaved by the prohead protease.
View Article and Find Full Text PDFThe T4 TerL Prohead Packaging Motor Does Not Drive DNA Translocation by a Proposed Dehydration Mechanism.
Viruses
May 2020
Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD 21201, USA.
A "DNA crunching" linear motor mechanism that employs a grip-and-release transient spring like compression of B- to A-form DNA has been found in our previous studies. Our FRET measurements in vitro show a decrease in distance from TerL to portal during packaging; furthermore, there is a decrease in distance between closely positioned dye pairs in the Y-stem of translocating Y-DNA that conforms to B- and A- structure. In normal translocation into the prohead the TerL motor expels all B-form tightly binding YOYO-1 dye that cannot bind A-form.
View Article and Find Full Text PDFA viral small terminase subunit (TerS) twin ring pac synapsis DNA packaging model is supported by fluorescent fusion proteins.
Virology
October 2019
Department of Biochemistry and Molecular Biology, University of Maryland School of Medicine, Baltimore, MD, 21201, USA. Electronic address:
A bacteriophage T4 DNA "synapsis model" proposes that the bacteriophage T4 terminase small subunit (TerS) apposes two pac site containing dsDNA homologs to gauge concatemer maturation adequate for packaging initiation. N-terminus, C-terminus, or both ends modified fusion Ter S proteins retain function. Replacements of the TerS gene in the T4 genome with fusion genes encoding larger (18-45 kDa) TerS-eGFP and TerS-mCherry fluorescent fusion proteins function without significant change in phenotype.
View Article and Find Full Text PDFGlobal Proteomic Profiling of Infection by a Giant Phage.
J Virol
March 2019
Thomas H. Gosnell School of Life Sciences, Rochester Institute of Technology, Rochester, New York, USA
The 240-kb phage SPN3US genome encodes 264 gene products, many of which are functionally uncharacterized. We have previously used mass spectrometry to define the proteomes of wild-type and mutant forms of the SPN3US virion. In this study, we sought to determine whether this technique was suitable for the characterization of the SPN3US proteome during liquid infection.
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