Faculty Opinions recommendation of Topological friction strongly affects viral DNA ejection.

Author(s):  
Michael B Sherman
Keyword(s):  
2007 ◽  
Vol 189 (15) ◽  
pp. 5542-5549 ◽  
Author(s):  
Martín Alcorlo ◽  
Víctor González-Huici ◽  
José M. Hermoso ◽  
Wilfried J. J. Meijer ◽  
Margarita Salas

ABSTRACT It is becoming clear that in vivo phage DNA ejection is not a mere passive process. In most cases, both phage and host proteins seem to be involved in pulling at least part of the viral DNA inside the cell. The DNA ejection mechanism of Bacillus subtilis bacteriophage φ29 is a two-step process where the linear DNA penetrates the cell with a right-left polarity. In the first step ∼65% of the DNA is pushed into the cell. In the second step, the remaining DNA is actively pulled into the cytoplasm. This step requires protein p17, which is encoded by the right-side early operon that is ejected during the first push step. The membrane protein p16.7, also encoded by the right-side early operon, is known to play an important role in membrane-associated phage DNA replication. In this work we show that, in addition, p16.7 is required for efficient execution of the second pull step of DNA ejection.


Nanoscale ◽  
2018 ◽  
Vol 10 (4) ◽  
pp. 1898-1904 ◽  
Author(s):  
Miklós S. Z. Kellermayer ◽  
Zsuzsanna Vörös ◽  
Gabriella Csík ◽  
Levente Herényi

Mechanical load on the T7 capsid triggers the ejection of its DNA.


2017 ◽  
Vol 1861 (3) ◽  
pp. 664-672 ◽  
Author(s):  
Isaac Santos-Pérez ◽  
Hanna M. Oksanen ◽  
Dennis H. Bamford ◽  
Felix M. Goñi ◽  
David Reguera ◽  
...  
Keyword(s):  

2013 ◽  
Vol 110 (50) ◽  
pp. 20081-20086 ◽  
Author(s):  
D. Marenduzzo ◽  
C. Micheletti ◽  
E. Orlandini ◽  
D. W. Sumners
Keyword(s):  

2017 ◽  
Vol 95 (5) ◽  
Author(s):  
Nicholas Keller ◽  
Zachary T. Berndsen ◽  
Paul J. Jardine ◽  
Douglas E. Smith

2017 ◽  
Vol 112 (3) ◽  
pp. 216a
Author(s):  
Miklós S. Kellermayer ◽  
Zsuzsanna Vörös ◽  
Gabriella Csík ◽  
Levente Herényi

Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.


2010 ◽  
Vol 34 (8) ◽  
pp. S60-S60
Author(s):  
Yuning Sun ◽  
Fang Li ◽  
Jianming Qiu ◽  
Xiaohong Lu

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