Production of unstable proteins through the formation of stable core complexes

Nicolas Levy, Sylvia Eiler, Karine Pradeau-Aubreton, Benoit Maillot, François Stricher and Marc Ruff ()
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Nicolas Levy: IGBMC, UDS, CNRS, INSERM
Sylvia Eiler: IGBMC, UDS, CNRS, INSERM
Karine Pradeau-Aubreton: IGBMC, UDS, CNRS, INSERM
Benoit Maillot: IGBMC, UDS, CNRS, INSERM
François Stricher: IGBMC, UDS, CNRS, INSERM
Marc Ruff: IGBMC, UDS, CNRS, INSERM

Nature Communications, 2016, vol. 7, issue 1, 1-9

Abstract: Abstract Purification of proteins that participate in large transient complexes is impeded by low amounts, heterogeneity, instability and poor solubility. To circumvent these difficulties we set up a methodology that enables the production of stable complexes for structural and functional studies. This procedure is benchmarked and applied to two challenging protein families: the human steroid nuclear receptors (SNR) and the HIV-1 pre-integration complex. In the context of transcriptional regulation studies, we produce and characterize the ligand-binding domains of the glucocorticoid nuclear receptor and the oestrogen receptor beta in complex with a TIF2 (transcriptional intermediary factor 2) domain containing the three SNR-binding motifs. In the context of retroviral integration, we demonstrate the stabilization of the HIV-1 integrase by formation of complexes with partner proteins and DNA. This procedure provides a powerful research tool for structural and functional studies of proteins participating in non-covalent macromolecular complexes.

Date: 2016
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DOI: 10.1038/ncomms10932

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