Identification of candidates for interacting partners of the tail domain of DcNMCP1, a major component of the Daucus carota nuclear lamina-like structure
| العنوان: | Identification of candidates for interacting partners of the tail domain of DcNMCP1, a major component of the Daucus carota nuclear lamina-like structure |
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| المؤلفون: | Daisuke Tsugama, Kaien Fujino, Ryota Mochizuki, Michihiro Yamazaki, Kiyoshi Masuda |
| المصدر: | Nucleus |
| بيانات النشر: | Taylor & Francis, 2017. |
| سنة النشر: | 2017 |
| مصطلحات موضوعية: | 0301 basic medicine, genetic structures, Biology, Protein–protein interaction, protein-protein interaction, 03 medical and health sciences, Protein Domains, medicine, Inner membrane, Nuclear membrane, Nuclear protein, transcription factor, Original Research, Plant Proteins, Genetics, Nuclear Lamina, lamina-like structure, plants, Nuclear cap-binding protein complex, Cell Biology, Nuclear matrix, Cell biology, Daucus carota, nuclear membrane, Protein Transport, 030104 developmental biology, medicine.anatomical_structure, Nuclear lamina, chromatin, sense organs, actin, Lamin, Protein Binding |
| الوصف: | NMCP/CRWN (NUCLEAR MATRIX CONSTITUENT PROTEIN/CROWDED NUCLEI) is a major component of a protein fibrous meshwork (lamina-like structure) on the plant inner nuclear membrane. NMCP/CRWN contributes to regulating nuclear shape and nuclear functions. An NMCP/CRWN protein in Daucus carota (DcNMCP1) is localized to the nuclear periphery in interphase cells, and surrounds chromosomes in cells in metaphase and anaphase. The N-terminal region and the C-terminal region of DcNMCP1 are both necessary for localizing DcNMCP1 to the nuclear periphery. Here candidate interacting partners of the amino acid position 975–1053 of DcNMCP1 (T975–1053), which is present in the C-terminal region and contains a conserved sequence that plays a role in localizing DcNMCP1 to the nuclear periphery, are screened for. Arabidopsis thaliana nuclear proteins were subjected to far-Western blotting with GST-fused T975–1053 as a probe, and signals were detected at the positions corresponding to ∼70, ∼40, and ∼18 kDa. These ∼70, ∼40, and ∼18 kDa nuclear proteins were identified by mass spectrometry, and subjected to a yeast 2-hybrid (Y2H) analysis with T975–1053 as bait. In this analysis, the ∼40 kDa protein ARP7, which is a nuclear actin-related protein possibly involved in regulating chromatin structures, was confirmed to interact with T975–1053. Independently of the far-Western blotting, a Y2H screen was performed using T975–1053 as bait. Targeted Y2H assays confirmed that 3 proteins identified in the screen, MYB3, SINAT1, and BIM1, interact with T975–1053. These proteins might have roles in NMCP/CRWN protein-mediated biologic processes. |
| اللغة: | English |
| تدمد: | 1949-1042 1949-1034 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67963625a8d7b78fe9ddf735db71037dTest http://europepmc.org/articles/PMC5499906Test |
| حقوق: | OPEN |
| رقم الانضمام: | edsair.doi.dedup.....67963625a8d7b78fe9ddf735db71037d |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 19491042 19491034 |
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