Architecture of the high mobility group nucleosomal protein 2-nucleosome complex as revealed by methyl-based NMR

Hidenori Kato, Hugo Van Ingen, Bing-Rui Zhou, Hanqiao Feng, Michael Bustin, Lewis E Kay, Yawen Bai

Research output: Contribution to journalArticleAcademicpeer-review


Chromatin structure and function are regulated by numerous proteins through specific binding to nucleosomes. The structural basis of many of these interactions is unknown, as in the case of the high mobility group nucleosomal (HMGN) protein family that regulates various chromatin functions, including transcription. Here, we report the architecture of the HMGN2-nucleosome complex determined by a combination of methyl-transverse relaxation optimized nuclear magnetic resonance spectroscopy (methyl-TROSY) and mutational analysis. We found that HMGN2 binds to both the acidic patch in the H2A-H2B dimer and to nucleosomal DNA near the entry/exit point, "stapling" the histone core and the DNA. These results provide insight into how HMGNs regulate chromatin structure through interfering with the binding of linker histone H1 to the nucleosome as well as a structural basis of how phosphorylation induces dissociation of HMGNs from chromatin during mitosis. Importantly, our approach is generally applicable to the study of nucleosome-binding interactions in chromatin.
Original languageEnglish
Pages (from-to)12283-12288
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number30
Publication statusPublished - 26 Jul 2011
Externally publishedYes


  • DNA
  • high mobility group nucleosomal protein 2
  • histone H1
  • nuclear protein
  • unclassified drug
  • article
  • chromatin structure
  • nucleosome
  • priority journal
  • protein DNA binding
  • protein structure


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