globalchange  > 气候变化与战略
DOI: 10.1073/pnas.2010000117
论文题名:
Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments
作者: Sysoev V.O.; Kato M.; Sutherland L.; Hu R.; McKnight S.L.; Murray D.T.
刊名: Proceedings of the National Academy of Sciences of the United States of America
ISSN: 0027-8424
出版年: 2020
卷: 117, 期:38
起始页码: 23510
结束页码: 23518
语种: 英语
英文关键词: Cross-beta polymerization ; Intermediate filaments ; Low-complexity proteins ; Solid-state NMR
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
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.
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资源类型: 期刊论文
标识符: http://119.78.100.158/handle/2HF3EXSE/163390
Appears in Collections:气候变化与战略

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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

Recommended Citation:
Sysoev V.O.,Kato M.,Sutherland L.,et al. Dynamic structural order of a low-complexity domain facilitates assembly of intermediate filaments[J]. Proceedings of the National Academy of Sciences of the United States of America,2020-01-01,117(38)
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