AI Article Synopsis
- CENP-A, a variant of histone H3, forms nucleosomes that help identify centromere locations and have a distinct shape compared to traditional H3 nucleosomes.
- The research uses single-molecule FRET to show that these shape changes primarily result from the lateral sliding of DNA gyres within the nucleosome.
- The centromere protein CENP-C binds to CENP-A nucleosomes, reshaping them and aligning the DNA to resemble standard H3 nucleosomes, highlighting the role of external proteins in influencing nucleosome structure and centromere inheritance.
Article Abstract
The histone H3 variant CENP-A is incorporated into nucleosomes that mark centromere location. We have recently reported that CENP-A nucleosomes, compared with their H3 counterparts, confer an altered nucleosome shape. Here, using a single-molecule fluorescence resonance energy transfer (FRET) approach with recombinant human histones and centromere DNA, we found that the nucleosome shape change directed by CENP-A is dominated by lateral passing of two DNA gyres (gyre sliding). A nonhistone centromere protein, CENP-C, binds and reshapes the nucleosome, sliding the DNA gyres back to positions similar to those in canonical nucleosomes containing conventional histone H3. The model that we generated to explain the CENP-A-nucleosome transition provides an example of a shape change imposed by external binding proteins and has notable implications for understanding of the epigenetic basis of the faithful inheritance of centromere location on chromosomes.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4893769 | PMC |
| http://dx.doi.org/10.1038/nsmb.3175 | DOI Listing |
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