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. 2017 Dec 5;12(12):e0189040. doi: 10.1371/journal.pone.0189040

Fig 6. Purified recombinant H1.0 and its domains are functional.

Fig 6

(A) SDS—PAGE analysis of purified proteins used for in vitro assays. Protein samples were analysed using 17% SDS—PAGE gels. Proteins were visualized by staining with SimplyBlue SafeStain. PageRuler Unstained Protein Ladder, Thermo Scientific, was used as protein marker. (B) Native PAGE of complex formation between histone chaperone Nap1 and H1 histone or its domains. H2AH2B histone dimer was used as a control for Nap1 binding. A histone chaperone:histone complex migrates slower compared to the histone chaperone alone. Several slower migrating bands can be observed in native polyacrylamide gels, indicative of the formation of higher order association states, typical for Nap1 chaperone. (C) Native PAGE of complex formation between DNA and H1 histone or its domains. H2AH2B histone dimer was used as a control for DNA binding. DNA:histone complex migrates slower compared to DNA. The complexes were visualized by SyberGold. (D) GST pull-down assays using GST-H1.0 and NCP. The proteins were visualized by Simply Blue SafeStain.