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. 2015 Oct 25;43(22):10963–10974. doi: 10.1093/nar/gkv1011

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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 5. — Assembly pathway of the U4/U6 di-snRNP in vitro. First, the Sm, LSm and Snu13 proteins bind independently and with high affinity to the U4 and U6 snRNAs. Subsequent assembly of the full complex may progress through binding of Prp31 followed by Prp3/4 (top pathway) or through Prp3/4 binding followed by Prp31 (bottom pathway). Binding of Prp31 stabilizes a conformation of the 5′ stem-loop closer to Stem II, whereas binding of Prp3/4 stabilizes a conformation of the 5′ stem-loop closer to Stem I. In the fully assembled complex the 5′ stem-loop returns to its initial orientation.