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Efficient purification of chromatin architectural proteins: histones, HMGB proteins and FKBP3 (FKBP25) immunophilin

DOI: 10.1039/c2ra21758a DOI Help

Authors: Larus E. Foulger (Liverpool John Moores University) , Connie Goh Then Sin (Aston University) , Q. Q. Zhuang (Liverpool John Moores University) , Hugh Smallman (Liverpool John Moores University) , James M. Nicholson (Diamond Light Source) , Stanley J. Lambert (Liverpool John Moores University) , Colin D. Reynolds (Liverpool John Moores University) , Mark J. Dickman (University of Sheffield) , Christopher M. Wood (Liverpool John Moores University) , John P. Baldwin (Liverpool John Moores University) , Katie Evans (Liverpool John Moores University)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Rsc Advances , VOL 2 (28)

State: Published (Approved)
Published: September 2012

Abstract: A two-step process of high ionic strength lysis of chicken erythrocyte cell nuclei followed by cation-exchange chromatography has separated at very high yield all the histone and HMGB (high-mobility group B) nuclear proteins, except the less-soluble histone tetramers. Surprisingly high yields of the nuclear immunophilin FKBP3 (FKBP25) and Hsp70 (heat-shock protein 70) co-fractionate with HMGB1 and HMGB3. Furthermore, these proteins can be separated by anion-exchange chromatography. The purified nuclear proteins retain their native, post-translational modification (PTM) marks, including those associated with chromatin-fibre remodelling. These marks are intimately associated with the control of the cell cycle. The methods herein are therefore of value for targeting these and other nuclear proteins for future proteomic studies in healthy and diseased cells.

Subject Areas: Chemistry


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Added On: 02/03/2016 11:09

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