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Integrative Structural Investigation on the Architecture of Human Importin4_Histone H3/1-14_Asf1a Complex and Its Histone H3 Tail Binding
Korea Adv Inst Sci & Technol, Canc Metastasis Control Ctr, Dept Biol Sci, Daejeon 34141, South Korea..
Univ Calif San Francisco, Calif Inst Quantitat Biosci, Dept Bioengn & Therapeut Sci, Dept Pharmaceut Chem, San Francisco, CA 94158 USA..
Univ Michigan, Sch Med, Dept Biol Chem, 1150 W Med Ctr Dr,SPC 5606, Ann Arbor, MI 48109 USA..
Korea Adv Inst Sci & Technol, Canc Metastasis Control Ctr, Dept Biol Sci, Daejeon 34141, South Korea..
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2018 (English)In: Journal of Molecular Biology, ISSN 0022-2836, E-ISSN 1089-8638, Vol. 430, no 6, p. 822-841Article in journal (Refereed) Published
Abstract [en]

Importin4 transports histone H3/H4 in complex with Asf1a to the nucleus for chromatin assembly. Importin4 recognizes the nuclear localization sequence located at the N-terminal tail of histones. Here, we analyzed the structures and interactions of human Importin4, histones and Asf1a by cross-linking mass spectrometry, X-ray crystallography, negative-stain electron microscopy, small-angle X-ray scattering and integrative modeling. The cross-linking mass spectrometry data showed that the C-terminal region of Importin4 was extensively cross-linked with the histone H3 tail. We determined the crystal structure of the C-terminal region of Importin4 bound to the histone H3 peptide, thus revealing that the acidic patch in Importin4 accommodates the histone H3 tail, and that histone H3 Lys14 contributes to the interaction with Importin4. In addition, we show that Asf1a modulates the binding of histone H3/H4 to Importin4. Furthermore, the molecular architecture of the Importin4_histone H3/H4_Asf1a complex was produced through an integrative modeling approach. Overall, this work provides structural insights into how Importin4 recognizes histones and their chaperone complex.

Place, publisher, year, edition, pages
Academic Press, 2018. Vol. 430, no 6, p. 822-841
National Category
Biochemistry and Molecular Biology
Identifiers
URN: urn:nbn:se:kth:diva-226795DOI: 10.1016/j.jmb.2018.01.015ISI: 000429512800006PubMedID: 29408485Scopus ID: 2-s2.0-85042167090OAI: oai:DiVA.org:kth-226795DiVA, id: diva2:1209179
Funder
EU, European Research Council, 670821
Note

QC 20180522

Available from: 2018-05-22 Created: 2018-05-22 Last updated: 2018-05-22Bibliographically approved

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Hebert, Hans

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