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-Structure paper
タイトル | Diverse cytomotive actins and tubulins share a polymerization switch mechanism conferring robust dynamics. |
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ジャーナル・号・ページ | Sci Adv, Vol. 9, Issue 13, Page eadf3021, Year 2023 |
掲載日 | 2023年3月29日 |
著者 | James Mark Wagstaff / Vicente José Planelles-Herrero / Grigory Sharov / Aisha Alnami / Frank Kozielski / Emmanuel Derivery / Jan Löwe / |
PubMed 要旨 | Protein filaments are used in myriads of ways to organize other molecules within cells. Some filament-forming proteins couple the hydrolysis of nucleotides to their polymerization cycle, thus ...Protein filaments are used in myriads of ways to organize other molecules within cells. Some filament-forming proteins couple the hydrolysis of nucleotides to their polymerization cycle, thus powering the movement of other molecules. These filaments are termed cytomotive. Only members of the actin and tubulin protein superfamilies are known to form cytomotive filaments. We examined the basis of cytomotivity via structural studies of the polymerization cycles of actin and tubulin homologs from across the tree of life. We analyzed published data and performed structural experiments designed to disentangle functional components of these complex filament systems. Our analysis demonstrates the existence of shared subunit polymerization switches among both cytomotive actins and tubulins, i.e., the conformation of subunits switches upon assembly into filaments. These cytomotive switches can explain filament robustness, by enabling the coupling of kinetic and structural polarities required for cytomotive behaviors and by ensuring that single cytomotive filaments do not fall apart. |
リンク | Sci Adv / PubMed:36989372 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.6 - 3.8 Å |
構造データ | EMDB-14147, PDB-7quc: EMDB-14148, PDB-7qud: EMDB-14150, PDB-7qup: EMDB-14151, PDB-7quq: |
化合物 | ChemComp-GTP: ChemComp-MG: ChemComp-GDP: ChemComp-G2P: |
由来 |
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キーワード | CELL CYCLE / Cytyoskeleton / microtubules / cytomotive filaments / tubulin-like |