Work

The ATPase of the phi29 DNA packaging motor is a member of the hexameric AAA+ superfamily

Year: 2013

Type: article

Abstract: The AAA+ superfamily of proteins is a class of motor ATPases performing a wide range of functions that typically exist as hexamers. The ATPase of phi29 DNA packaging motor has long been a subject of debate in terms of stoichiometry and mechanism of action. Here, we confirmed the stoichiometry of phi29 motor ATPase to be a hexamer and provide data suggesting that the phi29 motor ATPase is a member of the classical hexameric AAA+ superfamily. Native PAGE, EMSA, capillary electrophoresis, ATP titration, and binomial distribution assay show that the ATPase is a hexamer. Mutations in the known Walker motifs of the ATPase validated our previous assumptions that the protein exists as another member of this AAA+ superfamily. Our data also supports the finding that the phi29 DNA packaging motor uses a revolution mechanism without rotation or coiling (Schwartz et al., this issue).

Source: Virology

DOI: 10.1016/j.virol.2013.04.004

Authors: Chad Schwartz, Gian Marco De Donatis, Huaming Fang, Peixuan Guo

Institutions: University of Kentucky, Markey Cancer Center

Language: English

Topic: Bacteriophages and microbial interactions

Subfield: Ecology

Field: Environmental Science

Domain: Physical Sciences

Open Access status: hybrid

Estimated APC paid: $3,160

Funders: Korea Transport Institute, National Institutes of Health, National Cancer Institute, National Institute of Biomedical Imaging and Bioengineering