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. 2015 Mar 25;10(3):e0120268. doi: 10.1371/journal.pone.0120268

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© 2015 Genzor, Bortvin

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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Fig 5 — (A) The secondary structure of a conserved fragment of L1_Md_F2 element from chromosome 10 enriched in MAEL immunoprecipitates determined using combination of covariance and thermodynamic analyses. (B) MAEL HMG-box domain forms strong multi-protein complex with 277-nt fragment and binds weakly to shorter fragments (200-nt, 149-nt) of the same RNA. This suggests a requirement for complex tertiary structures in long RNAs for strong binding to the MAEL HMG-box domain. (C) MAEL HMG-box domain does not bind long RNAs originating from regions not enriched in MAEL immunoprecipitates.