气候变化领域集成服务门户(CCPortal): Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments

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DOI	10.1073/pnas.2010000117
	Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments
	Sysoev V.O.; Kato M.; Sutherland L.; Hu R.; McKnight S.L.; Murray D.T.
发表日期	2020
ISSN	0027-8424
起始页码	23510
结束页码	23518
卷号	117 期号:38
英文摘要	The coiled-coil domains of intermediate filament (IF) proteins are flanked by regions of low sequence complexity. Whereas IF coiledcoil domains assume dimeric and tetrameric conformations on their own, maturation of eight tetramers into cylindrical IFs is dependent on either "head" or "tail" domains of low sequence complexity. Here we confirm that the tail domain required for assembly of Drosophila Tm1-I/C IFs functions by forming labile cross-β interactions. These interactions are seen in polymers made from the tail domain alone, as well as in assembled IFs formed by the intact Tm1-I/C protein. The ability to visualize such interactions in situ within the context of a discrete cellular assembly lends support to the concept that equivalent interactions may be used in organizing other dynamic aspects of cell morphology. © 2020 National Academy of Sciences. All rights reserved.
英文关键词	Cross-beta polymerization; Intermediate filaments; Low-complexity proteins; Solid-state NMR
语种	英语
scopus关键词	tropomyosin; intermediate filament protein; amino terminal sequence; Article; beta sheet; carbon nuclear magnetic resonance; controlled study; Drosophila; electron microscopy; Escherichia coli; insensitive nuclei enhanced by polarization transfer; intermediate filament; nitrogen nuclear magnetic resonance; nonhuman; polarization; priority journal; protein assembly; protein conformation; protein interaction; animal; chemistry; metabolism; nuclear magnetic resonance; polymerization; ultrastructure; Animals; Drosophila; Intermediate Filament Proteins; Intermediate Filaments; Nuclear Magnetic Resonance, Biomolecular; Polymerization; Protein Conformation
来源期刊	Proceedings of the National Academy of Sciences of the United States of America
文献类型	期刊论文
条目标识符	http://gcip.llas.ac.cn/handle/2XKMVOVA/160220
作者单位	Sysoev, V.O., Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390, United States; Kato, M., Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390, United States, Institute for Quantum Life Science, National Institutes for Quantum and Radiological Science and Technology, Chiba, 263-8555, Japan; Sutherland, L., Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390, United States; Hu, R., Department of Chemistry, University of California, Davis, CA 95616, United States; McKnight, S.L., Department of Biochemistry, UT Southwestern Medical Center, Dallas, TX 75390, United States; Murray, D.T., Department of Chemistry, University of California, Davis, CA 95616, United States
推荐引用方式 GB/T 7714	Sysoev V.O.,Kato M.,Sutherland L.,et al. Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments[J],2020,117(38).
APA	Sysoev V.O.,Kato M.,Sutherland L.,Hu R.,McKnight S.L.,&Murray D.T..(2020).Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments.Proceedings of the National Academy of Sciences of the United States of America,117(38).
MLA	Sysoev V.O.,et al."Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments".Proceedings of the National Academy of Sciences of the United States of America 117.38(2020).