A viral genome packaging ring-ATPase is a flexibly coordinated pentamer

Li Dai, Digvijay Singh, Suoang Lu, Vishal I. Kottadiel, Reza Vafabakhsh, Marthandan Mahalingam, Yann R. Chemla (), Taekjip Ha () and Venigalla B. Rao ()
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Li Dai: The Catholic University of America
Digvijay Singh: Johns Hopkins University School of Medicine
Suoang Lu: University of Illinois at Urbana-Champaign
Vishal I. Kottadiel: The Catholic University of America
Reza Vafabakhsh: University of Illinois at Urbana-Champaign
Marthandan Mahalingam: The Catholic University of America
Yann R. Chemla: University of Illinois at Urbana-Champaign
Taekjip Ha: Johns Hopkins University School of Medicine
Venigalla B. Rao: The Catholic University of America

Nature Communications, 2021, vol. 12, issue 1, 1-14

Abstract: Abstract Multi-subunit ring-ATPases carry out a myriad of biological functions, including genome packaging in viruses. Though the basic structures and functions of these motors have been well-established, the mechanisms of ATPase firing and motor coordination are poorly understood. Here, using single-molecule fluorescence, we determine that the active bacteriophage T4 DNA packaging motor consists of five subunits of gp17. By systematically doping motors with an ATPase-defective subunit and selecting single motors containing a precise number of active or inactive subunits, we find that the packaging motor can tolerate an inactive subunit. However, motors containing one or more inactive subunits exhibit fewer DNA engagements, a higher failure rate in encapsidation, reduced packaging velocity, and increased pausing. These findings suggest a DNA packaging model in which the motor, by re-adjusting its grip on DNA, can skip an inactive subunit and resume DNA translocation, suggesting that strict coordination amongst motor subunits of packaging motors is not crucial for function.

Date: 2021
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DOI: 10.1038/s41467-021-26800-z

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