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. 2015 Dec 15;29(24):2576–2587. doi: 10.1101/gad.271528.115

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© 2015 Absmeier 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 4. — Model for the function of the Brr2 NTR. The NTR (magenta) serves to stably anchor Brr2 to the tri-snRNP and autoinhibits Brr2 in isolation and in the tri-snRNP, possibly avoiding engagement of off-target RNAs. Upon formation of a precatalytic spliceosome by association of the tri-snRNP with the A complex, conformational changes are required for Brr2 to engage U4 snRNA. To achieve productive Brr2-mediated tri-snRNP disruption (separation of U4/U6 and release of U4), parts of the Brr2 NTR need to fasten portions of the tri-snRNP that have to remain associated. After U4/U6 unwinding, the NTR might rebind the helicase region of Brr2 and thus shut off the enzyme again.