Literature DB >> 4074344

Binding of HMG14 non-histone protein to histones H2A, H2B, H1 and DNA in reconstituted chromatin.

E Espel, J Bernués, J A Pérez-Pons, E Querol.   

Abstract

The interaction between calf thymus HMG14 and rat liver chromatin components has been studied via reconstitution and chemical cross-linking. Selective labeling of HMG14 with photoactivable reversible heterobifunctional reagents has allowed a clear identification of the histones interacting with it (histones H2A, H2B and H1). These results are not dependent on whether the chromatin samples used were bulk chromatin, mononucleosomes, or core particles (for H2A and H2B). In addition to histone proteins, DNA also seems to be involved in HMG14 attachment to nucleosome.

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Year:  1985        PMID: 4074344     DOI: 10.1016/0006-291x(85)91910-2

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  4 in total

1.  The chromatin unfolding domain of chromosomal protein HMG-14 targets the N-terminal tail of histone H3 in nucleosomes.

Authors:  L Trieschmann; B Martin; M Bustin
Journal:  Proc Natl Acad Sci U S A       Date:  1998-05-12       Impact factor: 11.205

Review 2.  Regulation of chromatin structure and function by HMGN proteins.

Authors:  Yuri Postnikov; Michael Bustin
Journal:  Biochim Biophys Acta       Date:  2009-11-27

3.  HMGN1 modulates estrogen-mediated transcriptional activation through interactions with specific DNA-binding transcription factors.

Authors:  Nan Zhu; Ulla Hansen
Journal:  Mol Cell Biol       Date:  2007-10-15       Impact factor: 4.272

4.  A mitogen- and anisomycin-stimulated kinase phosphorylates HMG-14 in its basic amino-terminal domain in vivo and on isolated mononucleosomes.

Authors:  M J Barratt; C A Hazzalin; N Zhelev; L C Mahadevan
Journal:  EMBO J       Date:  1994-10-03       Impact factor: 11.598

  4 in total

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