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TitleNap1 and Kap114 co-chaperone H2A-H2B and facilitate targeted histone release in the nucleus.
Journal, issue, pagesJ Cell Biol, Vol. 224, Issue 1, Year 2025
Publish dateJan 6, 2025
AuthorsHo Yee Joyce Fung / Jenny Jiou / Ashley B Niesman / Natalia E Bernardes / Yuh Min Chook /
PubMed AbstractCore histones, synthesized and processed in the cytoplasm, must be chaperoned as they are transported into the nucleus for nucleosome assembly. The importin Kap114 transports H2A-H2B into the yeast ...Core histones, synthesized and processed in the cytoplasm, must be chaperoned as they are transported into the nucleus for nucleosome assembly. The importin Kap114 transports H2A-H2B into the yeast nucleus, where RanGTP facilitates histone release. Kap114 and H2A-H2B also bind the histone chaperone Nap1, but how Nap1 and Kap114 cooperate in transport and nucleosome assembly remains unclear. Here, biochemical and structural analyses show that Kap114, H2A-H2B, and a Nap1 dimer (Nap12) associate in the absence and presence of RanGTP to form equimolar complexes. A previous study had shown that RanGTP reduces Kap114's ability to chaperone H2A-H2B, but a new cryo-EM structure of the Nap12•H2A-H2B•Kap114•RanGTP complex explains how both Kap114 and Nap12 interact with H2A-H2B, restoring its chaperoning within the assembly while effectively depositing it into nucleosomes. Together, our results suggest that Kap114 and Nap12 provide a sheltered path that facilitates the transfer of H2A-H2B from Kap114 to Nap12, ultimately directing its specific deposition into nucleosomes.
External linksJ Cell Biol / PubMed:39601790 / PubMed Central
MethodsEM (single particle)
Resolution2.88 - 5.62 Å
Structure data

44095

9b23

EMDB-44095, PDB-9b23:
Cryo-EM structure of Nap1 core
Method: EM (single particle) / Resolution: 3.2 Å

44120

9b31

EMDB-44120, PDB-9b31:
Cryo-EM structure of yeast (Nap1)2-Kap114-H2A-H2B
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-44121: Local refined map for Nap1 region from (Nap1)2-Kap114-H2A-H2B structure
Method: EM (single particle) / Resolution: 4.84 Å

EMDB-44122: Consensus volume for (Nap1)2-Kap114-H2A-H2B
Method: EM (single particle) / Resolution: 3.2 Å

44136

9b3f

EMDB-44136, PDB-9b3f:
Cryo-EM structure of yeast (Nap1)2-H2A-H2B-Kap114
Method: EM (single particle) / Resolution: 3.54 Å

EMDB-44137: Locally refined map for Nap1 and H2A-H2B in (Nap1)2-H2A-H2B-Kap114 structure
Method: EM (single particle) / Resolution: 5.62 Å

EMDB-44140: Consensus volume for (Nap1)2-H2A-H2B-Kap114 structure
Method: EM (single particle) / Resolution: 3.54 Å

44141

9b3i

EMDB-44141, PDB-9b3i:
Cryo-EM structure of yeast (Nap1)2-H2A-H2B-Kap114-RanGTP
Method: EM (single particle) / Resolution: 2.88 Å

EMDB-44150: Local refined map for Nap1 and H2A-H2B region in (Nap1)2-H2A-H2B-Kap114-RanGTP structure
Method: EM (single particle) / Resolution: 3.97 Å

EMDB-44151: Consensus volume for (Nap1)2-H2A-H2B-Kap114-RanGTP
Method: EM (single particle) / Resolution: 2.88 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsCHAPERONE / Histone / TRANSPORT PROTEIN / Import / Nucleosome Assembly

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