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. 2015 Feb 26;43(5):2625–2637. doi: 10.1093/nar/gkv133

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 7. — Multiple mechanistic features contribute to Rat1-mediated RNAPII termination. Disruption of the RNAPII active center due to NTP misincorporation or specific sequences facilitated termination by Rat1/Rai1 in vitro. A specific interaction between Rat1/Rai1 and RNAPII is critical because Rat1/Rai1 cannot terminate Escherichia coli RNAP. Furthermore, Rat1 must degrade RNA transcripts to build up a driving force for termination. Thus, 5′-3′ exonuclease activity is essential for Rat1 not only to gain access to RNAPII but also to accumulate a sufficient driving force to execute termination. Active RNAPII, cyan; paused RNAPII, gray.