AI Article Synopsis
- CENP-A and CENP-B are key proteins at the centromere, crucial for chromosome structure, with CENP-A being a unique variant of histone H3 and CENP-B binding to a specific DNA sequence known as the CENP-B box.
- The study shows that centromere-specific nucleosomes form in vitro using these proteins, where CENP-A wraps around 147 base pairs of alpha-satellite DNA, similar to standard H3 nucleosomes.
- CENP-B influences the positioning of these nucleosomes by binding to the DNA when the CENP-B box is properly oriented, but does not change their rotational alignment, suggesting its role in the transl
Article Abstract
The human centromere proteins A (CENP-A) and B (CENP-B) are the fundamental centromere components of chromosomes. CENP-A is the centromere-specific histone H3 variant, and CENP-B specifically binds a 17-base pair sequence (the CENP-B box), which appears within every other alpha-satellite DNA repeat. In the present study, we demonstrated centromere-specific nucleosome formation in vitro with recombinant proteins, including histones H2A, H2B, H4, CENP-A, and the DNA-binding domain of CENP-B. The CENP-A nucleosome wraps 147 base pairs of the alpha-satellite sequence within its nucleosome core particle, like the canonical H3 nucleosome. Surprisingly, CENP-B binds to nucleosomal DNA when the CENP-B box is wrapped within the nucleosome core particle and induces translational positioning of the nucleosome without affecting its rotational setting. This CENP-B-induced translational positioning only occurs when the CENP-B box sequence is settled in the proper rotational setting with respect to the histone octamer surface. Therefore, CENP-B may be a determinant for translational positioning of the centromere-specific nucleosomes through its binding to the nucleosomal CENP-B box.
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