Characterization of the interaction between HMGB1 and H3-a possible means of positioning HMGB1 in chromatin.

Abstract:

:High mobility group protein B1 (HMGB1) binds to the internucleosomal linker DNA in chromatin and abuts the nucleosome. Bending and untwisting of the linker DNA results in transmission of strain to the nucleosome core, disrupting histone/DNA contacts. An interaction between H3 and HMGB1 has been reported. Here we confirm and characterize the interaction of HMGB1 with H3, which lies close to the DNA entry/exit points around the nucleosome dyad, and may be responsible for positioning of HMGB1 on the linker DNA. We show that the interaction is between the N-terminal unstructured tail of H3 and the C-terminal unstructured acidic tail of HMGB1, which are presumably displaced from DNA and the HMG boxes, respectively, in the HMGB1-nucleosome complex. We have characterized the interaction by nuclear magnetic resonance spectroscopy and show that it is extensive for both peptides, and appears not to result in the acquisition of significant secondary structure by either partner.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Watson M,Stott K,Fischl H,Cato L,Thomas JO

doi

10.1093/nar/gkt950

subject

Has Abstract

pub_date

2014-01-01 00:00:00

pages

848-59

issue

2

eissn

0305-1048

issn

1362-4962

pii

gkt950

journal_volume

42

pub_type

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