divalent metal- and high mobility group n protein-dependent nucleosome stability and conformation二价金属和高机动组n protein-dependent核小体的稳定性和构象.pdfVIP

SAGE-Hindawi Access to Research Journal of Nucleic Acids Volume 2010, Article ID 143890, 10 pages doi:10.4061/2010/143890 Research Article Divalent Metal- and High Mobility Group N Protein-Dependent Nucleosome Stability and Conformation Michelle S. Ong, Dileep Vasudevan, and Curt A. Davey Division of Structural and Computational Biology, School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, Singapore 637551 Correspondence should be addressed to Curt A. Davey, davey@.sg 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. High mobility group N proteins (HMGNs) bind specifically to the nucleosome core and act as chromatin unfolding and activating factors. Using an all-Xenopus system, we found that HMGN1 and HMGN2 binding to nucleosomes results in distinct ion- dependent conformation and stability. HMGN2 association with nucleosome core particle or nucleosomal array in the presence of divalent metal triggers a reversible transition to a species with much reduced electrophoretic mobility, consistent with a less compact state of the nucleosome. Residues outside of the nucleosome binding domain are required for the activity, which is also displayed by an HMGN1 truncation product lacking part of the regulatory domain. In addition, thermal denaturation assays show that the presence of 1 mM Mg2+ ¿ or Ca2+ gives a reduction in nucleosome core terminus stability, which is further substantially diminished by th