National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM141461
United States
National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)
GM069909
United States
Cancer Prevention and Research Institute of Texas (CPRIT)
RP170644
United States
Citation
Journal: Proc Natl Acad Sci U S A / Year: 2022 Title: Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex. Authors: Natália Elisa Bernardes / Ho Yee Joyce Fung / Yang Li / Zhe Chen / Yuh Min Chook / Abstract: IMPORTIN-4, the primary nuclear import receptor of core histones H3 and H4, binds the H3-H4 dimer and histone chaperone ASF1 prior to nuclear import. However, how H3-H3-ASF1 is recognized for ...IMPORTIN-4, the primary nuclear import receptor of core histones H3 and H4, binds the H3-H4 dimer and histone chaperone ASF1 prior to nuclear import. However, how H3-H3-ASF1 is recognized for transport cannot be explained by available crystal structures of IMPORTIN-4-histone tail peptide complexes. Our 3.5-Å IMPORTIN-4-H3-H4-ASF1 cryoelectron microscopy structure reveals the full nuclear import complex and shows a binding mode different from suggested by previous structures. The N-terminal half of IMPORTIN-4 clamps the globular H3-H4 domain and H3 αN helix, while its C-terminal half binds the H3 N-terminal tail weakly; tail contribution to binding energy is negligible. ASF1 binds H3-H4 without contacting IMPORTIN-4. Together, ASF1 and IMPORTIN-4 shield nucleosomal H3-H4 surfaces to chaperone and import it into the nucleus where RanGTP binds IMPORTIN-4, causing large conformational changes to release H3-H4-ASF1. This work explains how full-length H3-H4 binds IMPORTIN-4 in the cytoplasm and how it is released in the nucleus.
Macromolecule #2: GTP-binding nuclear protein GSP1/CNR1
Macromolecule
Name: GTP-binding nuclear protein GSP1/CNR1 / type: protein_or_peptide / ID: 2 Details: Truncated yeast Ran (residues 1-179) with the Q71L mutation Number of copies: 1 / Enantiomer: LEVO
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