Atomic resolution cryo-EM structure of a native-like CENP-A nucleosome aided by an antibody fragment

Bing-Rui Zhou, K. N. Sathish Yadav, Mario Borgnia, Jingjun Hong, Baohua Cao, Ada L. Olins, Donald E. Olins, Yawen Bai () and Ping Zhang ()
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Bing-Rui Zhou: National Institutes of Health
K. N. Sathish Yadav: National Institutes of Health
Mario Borgnia: National Institutes of Health
Jingjun Hong: National Institutes of Health
Baohua Cao: National Institutes of Health
Ada L. Olins: University of New England
Donald E. Olins: University of New England
Yawen Bai: National Institutes of Health
Ping Zhang: National Institutes of Health

Nature Communications, 2019, vol. 10, issue 1, 1-7

Abstract: Abstract Genomic DNA in eukaryotes is organized into chromatin through association with core histones to form nucleosomes, each distinguished by their DNA sequences and histone variants. Here, we used a single-chain antibody fragment (scFv) derived from the anti-nucleosome antibody mAb PL2-6 to stabilize human CENP-A nucleosome containing a native α-satellite DNA and solved its structure by the cryo-electron microscopy (cryo-EM) to 2.6 Å resolution. In comparison, the corresponding cryo-EM structure of the free CENP-A nucleosome could only reach 3.4 Å resolution. We find that scFv binds to a conserved acidic patch on the histone H2A-H2B dimer without perturbing the nucleosome structure. Our results provide an atomic resolution cryo-EM structure of a nucleosome and insight into the structure and function of the CENP-A nucleosome. The scFv approach is applicable to the structural determination of other native-like nucleosomes with distinct DNA sequences.

Date: 2019
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DOI: 10.1038/s41467-019-10247-4

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