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Journal of Nucleic Acids
Volume 2010, Article ID 143890, 10 pages
http://dx.doi.org/10.4061/2010/143890
Research Article

Divalent Metal- and High Mobility Group N Protein-Dependent Nucleosome Stability and Conformation

Division of Structural and Computational Biology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551

Received 14 July 2010; Accepted 29 September 2010

Academic Editor: Emery H. Bresnick

Copyright © 2010 Michelle S. Ong et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Supplementary Material

Supplementary Figures 1 to 5 entail EMSAs showing restriction digestion analysis to assess histone octamer saturation of 12-array, the HMGN binding-induced S2 transition is fully reversible, HMGN binding-induced transitions are not influenced by HMGN presence or introduction during nucleosome assembly and off-centered NCP undergoes a transition in the presence of divalent metal and associates with HMGN1 and HMGN1t to form an S2-like state.

  1. Supplementary Figures