Cofractionation of HMGB proteins with histone dimers |
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| Authors: | Qinqin Zhuang Hugh Smallman Stanley J Lambert Sirirath S Sodngam Colin D Reynolds Katie Evans Mark J Dickman John P Baldwin Christopher M Wood |
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| Institution: | 1. School of Pharmacy and Biomolecular Sciences, Liverpool John Moores University, Liverpool L3 3AF, UK;2. Natural Products Research Unit, Centre of Excellence for Innovation in Chemistry (PERCH-CIC), Department of Chemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand;3. ChELSI Institute, Department of Chemical and Biological Engineering, University of Sheffield, Sheffield S1 3JD, UK |
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| Abstract: | An effective and flexible method is presented that can be used to investigate cofractionation of groups of nuclear proteins. The method was used to analyze chromatin-related proteins, of which high-mobility group B (HMGB) proteins consistently cofractionated by cation-exchange chromatography with the histone dimer (H2A–H2B). This led to the hypothesis that the two form a complex, further suggested by gel filtration, in which the HMGBs with core histones eluted as a defined high-molecular-weight peak. A necessary requirement for further studying protein interactions is that the constituents are of the highest possible purity and the pure histone dimers and tetramers used in this study were derived from pure histone octamers with their native marks. There is a growing interest in protein–protein interactions and an increasing focus on protein-interaction domains: most frequently, pull-down assays are used to examine these. The technology presented here can provide an effective system that complements pull-down assays. |
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| Keywords: | Histone octamer Histone dimer Histone tetramer HMGB interactions Protein interaction domains Pull-down assays |
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