A programmable DNA origami nanospring that reveals force-induced adjacent binding of myosin VI heads.
Nat Commun
; 7: 13715, 2016 12 12.
Article
em En
| MEDLINE
| ID: mdl-27941751
ABSTRACT
Mechanosensitive biological nanomachines such as motor proteins and ion channels regulate diverse cellular behaviour. Combined optical trapping with single-molecule fluorescence imaging provides a powerful methodology to clearly characterize the mechanoresponse, structural dynamics and stability of such nanomachines. However, this system requires complicated experimental geometry, preparation and optics, and is limited by low data-acquisition efficiency. Here we develop a programmable DNA origami nanospring that overcomes these issues. We apply our nanospring to human myosin VI, a mechanosensory motor protein, and demonstrate nanometre-precision single-molecule fluorescence imaging of the individual motor domains (heads) under force. We observe force-induced transitions of myosin VI heads from non-adjacent to adjacent binding, which correspond to adapted roles for low-load and high-load transport, respectively. Our technique extends single-molecule studies under force and clarifies the effect of force on biological processes.
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Cadeias Pesadas de Miosina
/
Nanotecnologia
Limite:
Humans
Idioma:
En
Ano de publicação:
2016
Tipo de documento:
Article