Electron microscopic recording of myosin head power stroke in hydrated myosin filaments View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2015-10-26

AUTHORS

Haruo Sugi, Shigeru Chaen, Tsuyoshi Akimoto, Hiroki Minoda, Takuya Miyakawa, Yumiko Miyauchi, Masaru Tanokura, Seiryo Sugiura

ABSTRACT

Muscle contraction results from cyclic attachment and detachment between myosin heads and actin filaments, coupled with ATP hydrolysis. Despite extensive studies, however, the amplitude of myosin head power stroke still remains to be a mystery. Using the gas environmental chamber, we have succeeded in recording the power stroke of position-marked myosin heads in hydrated mixture of actin and myosin filaments in a nearly isometric condition, in which myosin heads do not produce gross myofilament sliding, but only stretch adjacent elastic structures. On application of ATP, individual myosin heads move by ~3.3 nm at the distal region, and by ~2.5 nm at the proximal region of myosin head catalytic domain. After exhaustion of applied ATP, individual myosin heads return towards their initial position. At low ionic strength, the amplitude of myosin head power stroke increases to >4 nm at both distal and proximal regions of myosin heads catalytic domain, being consistent with the report that the force generated by individual myosin heads in muscle fibers is enhanced at low ionic strength. The advantages of the present study over other in vitro motility assay systems, using myosin heads detached from myosin filaments, are discussed. More... »

PAGES

15700

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/srep15700

DOI

http://dx.doi.org/10.1038/srep15700

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013134011

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/26498981


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