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- W3135742268 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, by direct counting using single-molecule fluorescence, we have determined 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 count of active/inactive subunit(s), we found, unexpectedly, that the packaging motor can tolerate an inactive sub-unit. However, motors containing an inactive subunit(s) exhibit fewer DNA engagements, a higher failure rate in encapsidation, reduced packaging velocity, and increased pausing. These findings suggest a new packaging model in which the motor, by re-adjusting its grip on DNA, can skip an inactive subunit and resume DNA translocation, contrary to the prevailing notion of strict coordination amongst motor subunits of other packaging motors." @default.
- W3135742268 created "2021-03-15" @default.
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- W3135742268 date "2021-03-09" @default.
- W3135742268 modified "2023-10-16" @default.
- W3135742268 title "A viral genome packaging ring-ATPase is a flexibly coordinated pentamer" @default.
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- W3135742268 doi "https://doi.org/10.1101/2021.03.08.434477" @default.
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