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Unusual Nucleic Acid Binding Properties of Factor 2, an RNA Polymerase II Transcript Release Factor
Journal article   Open access   Peer reviewed

Unusual Nucleic Acid Binding Properties of Factor 2, an RNA Polymerase II Transcript Release Factor

Zhi Xie and David H Price
The Journal of biological chemistry, Vol.273(6), pp.3771-3777
02/06/1998
DOI: 10.1074/jbc.273.6.3771
PMID: 9452510
url
https://doi.org/10.1074/jbc.273.6.3771View
Published (Version of record) Open Access

Abstract

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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