Substrate interactions and promiscuity in a viral DNA packaging motor

K. Aathavan, Adam T. Politzer, Ariel Kaplan, Jeffrey R. Moffitt, Yann R. Chemla, Shelley Grimes, Paul J. Jardine, Dwight L. Anderson and Carlos Bustamante ()
Additional contact information
K. Aathavan: Biophysics Graduate Group,
Adam T. Politzer: Biophysics Graduate Group,
Ariel Kaplan: Jason L. Choy Laboratory of Single-Molecule Biophysics,
Jeffrey R. Moffitt: Jason L. Choy Laboratory of Single-Molecule Biophysics,
Yann R. Chemla: Jason L. Choy Laboratory of Single-Molecule Biophysics,
Shelley Grimes: Department of Diagnostic and Biological Sciences and Institute for Molecular Virology,
Paul J. Jardine: Department of Diagnostic and Biological Sciences and Institute for Molecular Virology,
Dwight L. Anderson: Department of Diagnostic and Biological Sciences and Institute for Molecular Virology,
Carlos Bustamante: Biophysics Graduate Group,

Nature, 2009, vol. 461, issue 7264, 669-673

Abstract: Viral packaging Viral packaging motors, multimeric ring-shaped ATPases of the ASCE superfamily, mediate filling of the capsid with the viral genome by translocating unidirectionally along nucleic acid in a nucleotide-dependent manner. Aathavan et al. use single-molecule approaches to determine how the motor protein interacts with the phosphate backbone of the nucleic acid during packing of the Bacillus subtilis bacteriophage ϕ29. They find that phosphate charges facilitate — but are not required for — translocation. In fact, the packaging motor is remarkably promiscuous, and even a non-biological polymer can be packaged. Normally, however, the motor interacts on one strand with a phosphate charge about every 10 base pairs.

Date: 2009
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DOI: 10.1038/nature08443

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