Literature DB >> 2335225

Interaction of histones H1 and H1(0) with superhelical and linear DNA.

J Yaneva1, J Zlatanova, E Paneva, L Srebreva, R Tsanev.   

Abstract

By using direct competition experiments, the binding of histone H1AB (a mixture of H1A and H1B) and H1(0) to superhelical and linear DNA forms was studied. Mouse liver H1 isohistones and plasmid p alpha GD containing part of the 5' flanking and part of the coding sequence of the mouse alpha-globin gene in pUC18 were used as partners in the binding reaction. The competition experiments were performed by direct mixing of the histone with labelled supercoiled DNA (at 125 mM NaCl and at a histone/DNA ratio of 1.0) and addition to the mixture of increasing amounts of cold competitor DNA, either supercoiled or linear. The radioactivity of the complex formed was determined by filter binding. The results show that both histones H1 and H1(0) posses a strong binding preference for supercoiled DNA forms. Thus, histone H1(0) resembles the regular somatic set of histone H1 and not the other differentiation-specific histone H5 studied thus far.

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Year:  1990        PMID: 2335225     DOI: 10.1016/0014-5793(90)81379-3

Source DB:  PubMed          Journal:  FEBS Lett        ISSN: 0014-5793            Impact factor:   4.124


  3 in total

Review 1.  DNA sequence specific interactions of histone H1.

Authors:  J Zlatanova; J Yaneva
Journal:  Mol Biol Rep       Date:  1991-02       Impact factor: 2.316

2.  Histone H1 preferentially binds to superhelical DNA molecules of higher compaction.

Authors:  M Ivanchenko; J Zlatanova; K van Holde
Journal:  Biophys J       Date:  1997-03       Impact factor: 4.033

3.  Histones H1 and H5 interact preferentially with crossovers of double-helical DNA.

Authors:  D Krylov; S Leuba; K van Holde; J Zlatanova
Journal:  Proc Natl Acad Sci U S A       Date:  1993-06-01       Impact factor: 11.205

  3 in total

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