Cited by 21Advanced Fluorescence Microscopy TechniquesCardiomyopathy and Myosin StudiesProtein Structure and Dynamics

ATP turnover by individual myosin molecules hints at two conformers of the myosin active site

Open access
Amrute-Nayak, Mamta, Lambeck, Katharina-Antonia, Radocaj, Ante, Huhnt, Helen Elisabeth, Scholz, Tim, Hahn, Nils, Tsiavaliaris, Georgios, Walter, Wilhelm J. +1 more·2014·Proceedings of the National Academy of Sciences

Abstract

Significance: Myosins use adenosine-5′-triphosphate (ATP) hydrolysis to drive motile functions, including muscle contraction. The main steps of ATP hydrolysis were previously identified by solution studies. Observing individual myosin molecules, one by one, interacting with fluorescently-labeled ATP, we found for one and the same myosin molecule two residence times for fluorescent ATP, a long lived, consistent with solution studies, and an unexpected short lived. Kinetic modeling suggests that this results from two active site conformers. In ensemble studies, generation of both dwell times from one myosin molecule had been indistinguishable from generation by a heterogeneous population of myosin molecules, demonstrating the power of molecule-by-molecule analysis to uncover previously undetected kinetic features and to distinguish, for example, different isoforms or mutant from wild-type molecules even in mixed populations.

Integrity signals

Registry

Crossref · 10.1073/pnas.1316390111

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37 of 37 references verified0 citation errors · 0 not checkable

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Authors
Amrute-Nayak, M., Lambeck, K.-A., Radocaj, A., Huhnt, H. E., Scholz, T., Hahn, N., Tsiavaliaris, G., Walter, W. J., & Brenner, B.
Affiliations
  • Department of Molecular and Cell Physiology and
  • Medizinische Hochschule Hannover (DE)
Venue
Proceedings of the National Academy of Sciences
Published
2014-02-03
Volume
111
Issue
7
Pages
2536-2541
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W2018967467
Cited by
21
References
37
Citations by year
2025: 4 · 2024: 4 · 2023: 1 · 2022: 1 · 2021: 1 · 2020: 2 · 2019: 2 · 2017: 2 · 2016: 2 · 2015: 1 · 2014: 1
FWCI
1.19
Type
journal article
Language
en
Open access
Locations
  • Proceedings of the National Academy of Sciences (publishedVersion)
  • Europe PMC (PubMed Central) (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biophysics › Advanced Fluorescence Microscopy Techniques
  • Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Cardiomyopathy and Myosin Studies
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
myosin, ATP turnover, chemo-mechanical coupling, ATPase kinetics, nucleotide binding, motor domain
MeSH terms
Adenosine Triphosphate, Computer Simulation, Hydrolysis, Kinetics, Microscopy, Fluorescence, Models, Chemical, Monte Carlo Method, Muscle Contraction, Myosins, Protein Conformation, Time Factors, Protein Isoforms

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