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J Biol Chem, Vol. 273, Issue 6, 3771-3777, February 6, 1998
From the Department of Biochemistry, University of Iowa, Iowa City,
Iowa 52242
Drosophila factor 2, an RNA
polymerase II transcript release factor, exhibits a
DNA-dependent ATPase activity (Xie, Z., and Price D. H. (1997) J. Biol. Chem. 272, 31902-31907). We
examined the nucleic acid requirement and found that only
double-stranded DNA (dsDNA) effectively activated the ATPase.
Single-stranded DNA (ssDNA) not only failed to activate the ATPase, but
suppressed the dsDNA-dependent ATPase. Gel mobility shift
assays showed that factor 2 formed stable complexes with dsDNA or ssDNA
in the absence of ATP. However, in the presence of ATP, the interaction
of factor 2 with dsDNA was destabilized, while the ssDNA-factor 2 complexes were not affected. The interaction of factor 2 with dsDNA was sensitive to increasing salt concentrations and was competed by ssDNA.
In both cases, loss of binding of factor 2 to dsDNA was mirrored by a
decrease in ATPase and transcript release activity, suggesting that the
interaction of factor 2 with dsDNA is important in coupling the ATPase
with the transcript release activity. Although the properties of factor
2 suggested that it might have helicase activity, we were unable to
detect any DNA unwinding activity associated with factor 2.
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