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. 2019 Aug;25(8):1020–1037. doi: 10.1261/rna.070649.119

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© 2019 Talkish et al.; Published by Cold Spring Harbor Laboratory Press for the RNA Society

This article, published in RNA, is available under a Creative Commons License (Attribution 4.0 International), as described at http://creativecommons.org/licenses/by/4.0/.

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FIGURE 6. — Disruption of the interaction between the UHM of Cus2 and the ULM of Hsh155 bypasses the essential ATP-dependent function of Prp5. The ULM of Hsh155 was mutated (R100D, W101A) in yeast strain DS4D (prp5Δ, cus2Δ, u2Δ; Perriman et al. 2003) harboring pRS317-CUS2, pRS315-U2, and pRS316-PRP5. The wild-type and hsh155^RW-DA mutant strains were then transformed with pRS314-prp5-GNT (left) and then plated on medium containing 5-FOA (right) to select for cells able to lose the pRS316-PRP5 plasmid.