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Expression of rat histone H1d in Escherichia coli and its purification

Srinivas Bharath, MM and Khadake, JR and Rao, MRS (1998) Expression of rat histone H1d in Escherichia coli and its purification. In: Protein Expression and Purification, 12 (01). pp. 38-44.

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Abstract

Histone H1 is involved in the folding of linear polynucleosomal filament into a 30-nm fiber. In an effort to understand the role of different domains of histone H1 in chromatin folding, we have now expressed rat histone H1d in Escherichia coli using pTrc99A expression vector by providing a 6-His tag at the C-terminus to facilitate its purification, The expressed protein histone H1d was purified from the soluble extract of E. coli by employing Ni2+ NTA-agarose and heparin-agarose chromatography. The recombinant histone H1d was shown to be authentic by its N-terminal amino acid analysis, its secondary structural characteristics, and its ability to (a) condense DNA and (b) bind specifically to synthetic four-way junction DNA

Item Type: Journal Article
Additional Information: Copyright of this article belongs to Elsevier Sciences.
Department/Centre: Division of Biological Sciences > Biochemistry
Date Deposited: 19 Jul 2009 06:39
Last Modified: 19 Sep 2010 05:24
URI: http://eprints.iisc.ernet.in/id/eprint/18642

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