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 Resjournal_title
Nucleic acids researchauthors
Watson M,Stott K,Fischl H,Cato L,Thomas JOdoi
10.1093/nar/gkt950subject
Has Abstractpub_date
2014-01-01 00:00:00pages
848-59issue
2eissn
0305-1048issn
1362-4962pii
gkt950journal_volume
42pub_type
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