CENP-C directs a structural transition of the CENP-A nucleosome mainly through sliding of DNA gyres
| Autor: | Michael Sennett, Tae Hee Lee, Jaehyoun Lee, Samantha J. Falk, Ben E. Black, Nikolina Sekulic |
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| Jazyk: | angličtina |
| Rok vydání: | 2016 |
| Předmět: |
0301 basic medicine
Models Molecular Chromosomal Proteins Non-Histone Centromere macromolecular substances Autoantigens Models Biological Article 03 medical and health sciences chemistry.chemical_compound Histone H3 Structural Biology Centromere Protein A Histone methylation Fluorescence Resonance Energy Transfer Nucleosome Humans Molecular Biology Genetics biology Linker DNA Nucleosomes 030104 developmental biology Histone chemistry biology.protein Biophysics DNA |
| Zdroj: | Nature structural & molecular biology |
| ISSN: | 1545-9985 1545-9993 |
| Popis: | The histone H3 variant, CENP-A, is incorporated into nucleosomes that mark centromere location. We recently reported that CENP-A confers an altered nucleosome shape relative to its counterparts containing conventional H3. Using a single molecule fluorescence resonance energy transfer (FRET) approach with recombinant human histones and centromere DNA, we now find that the nucleosome shape change that CENP-A directs is dominated by lateral passing of the two DNA gyres (gyre sliding). A non-histone centromere protein, CENP-C, binds to and reshapes the nucleosome, sliding the DNA gyres back to positions similar to those in canonical nucleosomes containing conventional histone H3. The model we generate to explain the CENP-A nucleosome transition provides an example of a shape change imposed by external binding proteins, and has important implications for understanding the epigenetic basis for the faithful inheritance of centromere location on the chromosome. |
| Databáze: | OpenAIRE |
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