دورية أكاديمية
أعرض في EDS

Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.

التفاصيل البيبلوغرافية
العنوان: Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.
المؤلفون: Bernardes NE; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390., Fung HYJ; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390., Li Y; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390., Chen Z; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390., Chook YM; Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75390.; Department of Biophysics, University of Texas Southwestern Medical Center, Dallas, TX 75390.
المصدر: Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 2022 Sep 20; Vol. 119 (38), pp. e2207177119. Date of Electronic Publication: 2022 Sep 14.
نوع المنشور: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: National Academy of Sciences Country of Publication: United States NLM ID: 7505876 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1091-6490 (Electronic) Linking ISSN: 00278424 NLM ISO Abbreviation: Proc Natl Acad Sci U S A Subsets: MEDLINE
أسماء مطبوعة: Original Publication: Washington, DC : National Academy of Sciences
مواضيع طبية MeSH: Histone Chaperones*/chemistry , Histones*/chemistry , Karyopherins*/chemistry , Membrane Transport Proteins*/chemistry , Molecular Chaperones*/chemistry , Saccharomyces cerevisiae Proteins*/chemistry, Cell Nucleus/metabolism ; Cryoelectron Microscopy ; Cytoplasm/metabolism ; Humans ; Protein Conformation ; Protein Multimerization
مستخلص: 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.
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معلومات مُعتمدة: R01 GM069909 United States GM NIGMS NIH HHS; R35 GM141461 United States GM NIGMS NIH HHS
فهرسة مساهمة: Keywords: histones; importin; karyopherins; nuclear import; nucleosome
المشرفين على المادة: 0 (ASF1 protein, S cerevisiae)
0 (Histone Chaperones)
0 (Histones)
0 (IPO4 protein, human)
0 (Karyopherins)
0 (Membrane Transport Proteins)
0 (Molecular Chaperones)
0 (Saccharomyces cerevisiae Proteins)
تواريخ الأحداث: Date Created: 20220914 Date Completed: 20220916 Latest Revision: 20230404
رمز التحديث: 20230404
مُعرف محوري في PubMed: PMC9499513
DOI: 10.1073/pnas.2207177119
PMID: 36103578
قاعدة البيانات: MEDLINE
الوصف
تدمد:1091-6490
DOI:10.1073/pnas.2207177119