Evidence for an electrostatic mechanism of force generation by the bacteriophage T4 DNA packaging motor

Amy D. Migliori, Nicholas Keller, Tanfis I. Alam, Marthandan Mahalingam, Venigalla B. Rao (), Gaurav Arya () and Douglas E. Smith ()
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Amy D. Migliori: University of California, 9500 Gilman Drive, La Jolla
Nicholas Keller: University of California, 9500 Gilman Drive, La Jolla
Tanfis I. Alam: The Catholic University of America, 620 Michigan Avenue NE
Marthandan Mahalingam: The Catholic University of America, 620 Michigan Avenue NE
Venigalla B. Rao: The Catholic University of America, 620 Michigan Avenue NE
Gaurav Arya: University of California, 9500 Gilman Drive, La Jolla
Douglas E. Smith: University of California, 9500 Gilman Drive, La Jolla

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: Abstract How viral packaging motors generate enormous forces to translocate DNA into viral capsids remains unknown. Recent structural studies of the bacteriophage T4 packaging motor have led to a proposed mechanism wherein the gp17 motor protein translocates DNA by transitioning between extended and compact states, orchestrated by electrostatic interactions between complimentarily charged residues across the interface between the N- and C-terminal subdomains. Here we show that site-directed alterations in these residues cause force dependent impairments of motor function including lower translocation velocity, lower stall force and higher frequency of pauses and slips. We further show that the measured impairments correlate with computed changes in free-energy differences between the two states. These findings support the proposed structural mechanism and further suggest an energy landscape model of motor activity that couples the free-energy profile of motor conformational states with that of the ATP hydrolysis cycle.

Date: 2014
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DOI: 10.1038/ncomms5173

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