期刊
SCIENCE
卷 331, 期 6013, 页码 80-83出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1197692
关键词
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资金
- Ministry of Education, Culture, Sports, Science and Technology of Japan (MEXT)
- Uehara Memorial Foundation
- Human Frontier Science Program
- Grants-in-Aid for Scientific Research [23121514, 23229003, 22501011] Funding Source: KAKEN
Formin homology proteins (formins) elongate actin filaments (F-actin) by continuously associating with filament tips, potentially harnessing actin-generated pushing forces. During this processive elongation, formins are predicted to rotate along the axis of the double helical F-actin structure (referred to here as helical rotation), although this has not yet been definitively shown. We demonstrated helical rotation of the formin mDia1 by single-molecule fluorescence polarization (FLP). FLP of labeled F-actin, both elongating and depolymerizing from immobilized mDia1, oscillated with a periodicity corresponding to that of the F-actin long-pitch helix, and this was not altered by actin-bound nucleotides or the actin-binding protein profilin. Thus, helical rotation is an intrinsic property of formins. To harness pushing forces from growing F-actin, formins must be anchored flexibly to cell structures.
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