دورية أكاديمية
Structure of IMPORTIN-4 bound to the H3-H4-ASF1 histone-histone chaperone complex.
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. |
References: | Proc Natl Acad Sci U S A. 1995 Feb 14;92(4):1237-41. (PMID: 7862667) Mol Syst Biol. 2011 Oct 11;7:539. (PMID: 21988835) Nat Methods. 2017 Mar;14(3):290-296. (PMID: 28165473) J Biol Chem. 2007 Jul 13;282(28):20142-50. (PMID: 17507373) Essays Biochem. 2019 Apr 23;63(1):29-43. (PMID: 31015382) J Biol Chem. 2012 Feb 24;287(9):6573-81. (PMID: 22228774) Sci Rep. 2017 Jun 8;7(1):3050. (PMID: 28596587) J Struct Biol. 2005 Oct;152(1):36-51. (PMID: 16182563) Acta Crystallogr D Biol Crystallogr. 2010 Feb;66(Pt 2):213-21. (PMID: 20124702) Nat Rev Mol Cell Biol. 2022 May;23(5):307-328. (PMID: 35058649) Exp Cell Res. 1998 Oct 10;244(1):206-17. (PMID: 9770363) Cell. 2004 Jan 9;116(1):51-61. (PMID: 14718166) Acta Crystallogr D Biol Crystallogr. 2011 Apr;67(Pt 4):235-42. (PMID: 21460441) Mol Cell. 2019 Mar 21;73(6):1191-1203.e6. (PMID: 30824373) J Comput Chem. 2004 Oct;25(13):1605-12. (PMID: 15264254) Elife. 2019 Mar 11;8:. (PMID: 30855230) J Biol Chem. 2016 Sep 30;291(40):21171-21183. (PMID: 27528606) Elife. 2017 Oct 16;6:. (PMID: 29035199) EMBO J. 2018 Oct 1;37(19):. (PMID: 30177573) Elife. 2015 Sep 08;4:. (PMID: 26349033) Nat Struct Mol Biol. 2010 Nov;17(11):1343-51. (PMID: 20953179) Cell Host Microbe. 2014 Aug 13;16(2):187-200. (PMID: 25121748) J Mol Biol. 2013 Jun 12;425(11):1852-1868. (PMID: 23541588) Proc Natl Acad Sci U S A. 2022 Sep 20;119(38):e2207177119. (PMID: 36103578) J Cell Biochem. 2001 Mar 26;81(2):333-46. (PMID: 11241673) Science. 2003 Nov 28;302(5650):1571-5. (PMID: 14645851) Nature. 1999 May 20;399(6733):230-7. (PMID: 10353245) EMBO Rep. 2001 Aug;2(8):690-6. (PMID: 11493596) Structure. 2016 Oct 4;24(10):1802-1809. (PMID: 27618664) J Mol Biol. 2018 Mar 16;430(6):822-841. (PMID: 29408485) Nature. 1997 Sep 18;389(6648):251-60. (PMID: 9305837) Cell. 2006 Nov 3;127(3):495-508. (PMID: 17081973) Anal Biochem. 2016 Mar 1;496:79-93. (PMID: 26739938) Mol Cell. 2010 Mar 12;37(5):736-43. (PMID: 20227376) Biochemistry. 2002 Jun 4;41(22):6955-66. (PMID: 12033928) Nat Rev Mol Cell Biol. 2017 Mar;18(3):141-158. (PMID: 28053344) J Biol Chem. 2011 May 20;286(20):17714-21. (PMID: 21454524) Biochemistry. 2003 Jun 10;42(22):6827-39. (PMID: 12779337) J Biol Chem. 2002 Jan 4;277(1):862-8. (PMID: 11694505) J Biol Chem. 2006 Apr 7;281(14):9287-96. (PMID: 16464854) Nat Commun. 2017 Oct 17;8(1):979. (PMID: 29042532) Nucleic Acids Res. 2014 Jul;42(Web Server issue):W320-4. (PMID: 24753421) Methods Enzymol. 2015;562:109-33. (PMID: 26412649) |
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 |
تدمد: | 1091-6490 |
---|---|
DOI: | 10.1073/pnas.2207177119 |