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. 2020 Nov 3;21:269. doi: 10.1186/s13059-020-02186-x

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© The Author(s) 2020

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 3 — SEELA binds K31 aa of histone H4 to promote the enhancer recognition of histone modification reader. a The reported RNA-binding proteomes identified histone H4 (P62805) as a RNA-binding protein candidate. b A schematic diagram shows the truncated fragments of H3 and H4 (left). RIP-qPCR for SEELA1-V1 pull-down by HA-tagged H3 and H4 sections in 293 T cells (right). The anti-HA antibody was used in RIP-qPCR assays. c–e The in vitro tRSA RNA pull-down assay with the purified different mutants of H4 proteins showed that the K31 aa of H4 mainly interacted with SEELA1-V1. f RIP-qPCR detection was used to assess the association of BRD4 with SEELA in MV4-11 and RS4;11 cells. Error bars reflect ± SEM in three independent experiments. An IgG antibody acted as a negative control. g Immunoblot detection of Flag-tagged BRD4 truncated fragments retrieved by in vitro-transcribed tRSA-tagged SEELA1-V1 from 293 T cell lysates. BRD4 (aa 1-1362, aa 1-722, and aa 466-1362) presented significantly higher enrichment of SEELA1-V1. h ChIP-qPCR assays after knocking down SEELA showed that the enrichments of BRD4 at the SEELA locus were downregulated in MV4-11. Error bars reflect ±SEM (*P < 0.05; **P < 0.01) in three independent experiments. An IgG antibody was used as a negative control in the ChIP assay. i A schematic diagram (left) shows stable overexpressed HA-tagged H4-full length or H4K31A into MV4-11 cells. The binding of SEELA is disrupted in H4K31A mutants, as a result, the missing of the SEELA-induced SERINC2 expression. The expression of SEELA and SERINC2 (right) were downregulated in H4K31A mutant expression cells versus that in the H4-full length expression cells. Error bars reflect ± SD (***P < 0.001) in three independent experiments