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

Nat Commun. 2021 Nov 12;12(1):6548. doi: 10.1038/s41467-021-26800-z.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Adenosine Triphosphatases / genetics
  • Adenosine Triphosphatases / metabolism*
  • Bacteriophage T4 / genetics
  • Bacteriophage T4 / metabolism
  • DNA Packaging / genetics
  • DNA Packaging / physiology
  • DNA, Viral / genetics
  • Viral Genome Packaging / genetics
  • Viral Genome Packaging / physiology*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism
  • Virus Assembly / genetics
  • Virus Assembly / physiology


  • DNA, Viral
  • Viral Proteins
  • Adenosine Triphosphatases