HMGA2 directly mediates chromatin condensation in association with neuronal fate regulation

Naohiro Kuwayama, Tomoya Kujirai, Yusuke Kishi, Rina Hirano, Kenta Echigoya, Lingyan Fang, Sugiko Watanabe, Mitsuyoshi Nakao, Yutaka Suzuki, Kei-ichiro Ishiguro, Hitoshi Kurumizaka () and Yukiko Gotoh ()
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Naohiro Kuwayama: The University of Tokyo
Tomoya Kujirai: The University of Tokyo
Yusuke Kishi: The University of Tokyo
Rina Hirano: The University of Tokyo
Kenta Echigoya: The University of Tokyo
Lingyan Fang: The University of Tokyo
Sugiko Watanabe: Kumamoto University
Mitsuyoshi Nakao: Kumamoto University
Yutaka Suzuki: The University of Tokyo
Kei-ichiro Ishiguro: Kumamoto University
Hitoshi Kurumizaka: The University of Tokyo
Yukiko Gotoh: The University of Tokyo

Nature Communications, 2023, vol. 14, issue 1, 1-18

Abstract: Abstract Identification of factors that regulate chromatin condensation is important for understanding of gene regulation. High-mobility group AT-hook (HMGA) proteins 1 and 2 are abundant nonhistone chromatin proteins that play a role in many biological processes including tissue stem-progenitor cell regulation, but the nature of their protein function remains unclear. Here we show that HMGA2 mediates direct condensation of polynucleosomes and forms droplets with nucleosomes. Consistently, most endogenous HMGA2 localized to transposase 5– and DNase I–inaccessible chromatin regions, and its binding was mostly associated with gene repression, in mouse embryonic neocortical cells. The AT-hook 1 domain was necessary for chromatin condensation by HMGA2 in vitro and in cellulo, and an HMGA2 mutant lacking this domain was defective in the ability to maintain neuronal progenitors in vivo. Intrinsically disordered regions of other proteins could substitute for the AT-hook 1 domain in promoting this biological function of HMGA2. Taken together, HMGA2 may regulate neural cell fate by its chromatin condensation activity.

Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42094-9

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DOI: 10.1038/s41467-023-42094-9

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