Literature DB >> 9357108

Purification of mouse H1 histones expressed in Escherichia coli.

S E Wellman1, Y Song, D Su, N M Mamoon.   

Abstract

We amplified the coding regions of the previously cloned H1 genes H1-1, H1 zero and H1t and inserted them into the expression vector pET-11d. The synthesis of the H1 histones can be induced in the appropriate strains of bacteria, and the H1 histones can be readily purified. We report detailed protocols for the purification of the expressed proteins using combinations of ion-exchange and reverse-phase HPLC. Sufficient amounts of each pure variant protein can be obtained for use in physical studies of H1-DNA interactions.

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Year:  1997        PMID： 9357108

Source DB:  PubMed          Journal:  Biotechnol Appl Biochem        ISSN： 0885-4513            Impact factor:   2.431


  4 in total

1.  Simplified method for recombinant linker histone H1 purification.

Authors:  Kayoko Hayashihara; Jordanka Zlatanova; Miroslav Tomschik
Journal:  Mol Biotechnol       Date:  2010-02       Impact factor: 2.695

2.  Chromatin condensing functions of the linker histone C-terminal domain are mediated by specific amino acid composition and intrinsic protein disorder.

Authors:  Xu Lu; Barbara Hamkalo; Missag H Parseghian; Jeffrey C Hansen
Journal:  Biochemistry       Date:  2009-01-13       Impact factor: 3.162

3.  Temperature and osmotic stress dependence of the thermodynamics for binding linker histone H10, Its carboxyl domain (H10-C) or globular domain (H10-G) to B-DNA.

Authors:  V R Machha; C G Mikek; S Wellman; E A Lewis
Journal:  Biochem Biophys Rep       Date:  2017-10-13

4.  Preparative two-step purification of recombinant H1.0 linker histone and its domains.

Authors:  Nives Ivic; Silvija Bilokapic; Mario Halic
Journal:  PLoS One       Date:  2017-12-05       Impact factor: 3.240
  4 in total

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