Abstract
Previously thought to function only as a passive portal for the phi29 DNA packaging motor, we demonstrate that the connector protein gene product 10 (gp10) exhibits significant ATPase activity. Bioluminescence assays have shown a concentration dependent decrease in available ATP after the addition of gp10. Also, enzyme-linked inorganic phosphate assays (ELIPA) have confirmed a time-dependent increase of phosphate in the presence of gp10 and ATP. Alone, gp10 acts as a slow ATPase with optimal hydrolysis of ATP occurring above room temperature at conditions native to the phi29 DNA motor. Overall increase of ATP hydrolysis in the system has been observed upon the addition of other phi29 motor components to gp10. Compared to gp16, a known ATPase, gp10 consumes ATP at a notably slower rate. Moreover, pRNA has shown no measurable ATPase activity. Combined, the phi29 motor assembly (i.e. gp10, gp16, and pRNA) has exhibited greater rates of ATP hydrolysis than any of these components independently.
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