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. 2021 Jul 23;14:34. doi: 10.1186/s13072-021-00409-4

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© The Author(s) 2021

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. 7 — Interaction network of Nrp1-HA and direct interaction of Nrp1 and Asf1. A Interaction network view of Nrp1-HA. The bait node is shown in purple. The distance and location of the prey node are shown according to their frequency and putative functions. B The structure of the Nrp1-Asf1 complex was predicted by Z-DOCK. The predicted structures and lipotropic property were viewed and rendered using PyMOL. C 12.5% SDS-PAGE analysis of His-Nrp1 and GST-Asf1. M: protein molecular weight markers; lane 1: purified His-Nrp1; lane 2: purified GST-Asf1; lane 3: purified GST. D Pull down assay confirms the interaction between Nrp1 and Asf1. Recombinant His-Nrp1 and GST-Asf1/GST were incubated with glutathione sepharose resin. Unbound proteins were washed off. The protein complexes were eluted and immunoblotted with anti-GST and anti-His antibodies, respectively