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. 2015 Jan 1;29(1):94–107. doi: 10.1101/gad.253070.114

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© 2015 Warkocki et al.; Published by Cold Spring Harbor Laboratory Press

This article is distributed exclusively by Cold Spring Harbor Laboratory Press for the first six months after the full-issue publication date (see http://genesdev.cshlp.org/site/misc/terms.xhtml). After six months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

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Figure 2. — The spliceosome is a potent stimulator of Prp2’s NTPase activity. (A) UTP hydrolysis was investigated by TLC and quantified by a PhosphorImager. UTP hydrolysis by the purified B^{act ΔPrp2
ΔSpp2} spliceosomes in either the absence [Act-wt B^act (bg)] or presence (Prp2 Act-wt B^act) of Prp2 or by Prp2 alone (Prp2) was determined. The amount of UTP hydrolyzed by Prp2 in spliceosomes (“UTP•spliceosome⁻¹”) and hydrolyzed by Prp2 in the absence of the spliceosome (Prp2) (“UTP•[Prp2]⁻¹”) is plotted as a function of time. Prp2 Act-wt B^act (−bg) was generated by subtracting the spliceosome alone [Act-wt B^act (bg)] values from those obtained with Prp2 Act-wt B^act. (B) Initial rate of UTP hydrolysis by Prp2 in spliceosomes within the first 2 min of the time course. Data points were analyzed by linear regression to derive the initial rate of Prp2-catalyzed UTP hydrolysis in the context of the spliceosome.