Structural Mechanism of TAF-Iβ Chaperone Function on Linker Histone H1.10

Haniqao Feng,Bing-Rui Zhou, Charles D Schwieters,Yawen Bai

Journal of Molecular Biology（2022）

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摘要

•Human linker histone isoform H1.10 and its chaperone TAF-Iβ form a 2:2 complex.•Structure of the H1.10-TAF-Iβ core complex from methyl NMR-spin label studies.•H1.10 interacts with TAF-Iβ mainly through electrostatic interactions.•TAF-Iβ functions as a chaperone by blocking the DNA binding sites of H1.10.

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关键词

Linker histone H1,TAF-Iβ,Histone chaperone,Methyl-TROSY,Spin label

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