Internal dynamics of F-actin and myosin subfragment-1 studied by quasielastic neutron scattering
Abstract
Various biological functions related to cell motility are driven by the interaction between the partner proteins, actin and myosin. To obtain insights into how this interaction occurs, the internal dynamics of F-actin and myosin subfragment-1 (S1) were characterized by the quasielastic neutron scattering measurements on the solution samples of F-actin and S1. Contributions of the internal motions of the proteins to the scattering spectra were separated from those of the global macromolecular diffusion. Analysis of the spectra arising from the internal dynamics showed that the correlation times of the atomic motions were about two times shorter for F-actin than for S1, suggesting that F-actin fluctuates more rapidly than S1. It was also shown that the fraction of the immobile atoms is larger for S1 than for F-actin. These results suggest that F-actin actively facilitates the binding of myosin by utilizing the more frequent conformational fluctuations than those of S1. - Highlights: • We studied the internal dynamics of F-actin and myosin S1 by neutron scattering. • The correlation times of the atomic motions were smaller for F-actin than for S1. • The fraction of the immobile atoms was also smaller for F-actin than for S1. • Our results suggest thatmore »
- Authors:
-
- Quantum Beam Science Center, Japan Atomic Energy Agency, Tokai, Ibaraki 319-1195 (Japan)
- Department of Biological Sciences, Graduate School of Science, Osaka University, Toyonaka, Osaka 560-0043 (Japan)
- Graduate School of Science, University of Hyogo, Kamigori-cho, Ako-gun, Hyogo 678-1297 (Japan)
- Neutron Science Section, J-PARC Center, Tokai, Ibaraki 319-1195 (Japan)
- Publication Date:
- OSTI Identifier:
- 22461997
- Resource Type:
- Journal Article
- Journal Name:
- Biochemical and Biophysical Research Communications
- Additional Journal Information:
- Journal Volume: 459; Journal Issue: 3; Other Information: Copyright (c) 2015 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
- Country of Publication:
- United States
- Language:
- English
- Subject:
- 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; ACTIN; ATOMS; BIOLOGICAL FUNCTIONS; CORRELATIONS; DIFFUSION; FLUCTUATIONS; INTERACTIONS; MOBILITY; MYOSIN; NEUTRON DIFFRACTION; QUASI-ELASTIC SCATTERING; SOLUTIONS; SPECTRA
Citation Formats
Matsuo, Tatsuhito, Arata, Toshiaki, Oda, Toshiro, Nakajima, Kenji, Ohira-Kawamura, Seiko, Kikuchi, Tatsuya, and Fujiwara, Satoru. Internal dynamics of F-actin and myosin subfragment-1 studied by quasielastic neutron scattering. United States: N. p., 2015.
Web. doi:10.1016/J.BBRC.2015.02.134.
Matsuo, Tatsuhito, Arata, Toshiaki, Oda, Toshiro, Nakajima, Kenji, Ohira-Kawamura, Seiko, Kikuchi, Tatsuya, & Fujiwara, Satoru. Internal dynamics of F-actin and myosin subfragment-1 studied by quasielastic neutron scattering. United States. https://doi.org/10.1016/J.BBRC.2015.02.134
Matsuo, Tatsuhito, Arata, Toshiaki, Oda, Toshiro, Nakajima, Kenji, Ohira-Kawamura, Seiko, Kikuchi, Tatsuya, and Fujiwara, Satoru. 2015.
"Internal dynamics of F-actin and myosin subfragment-1 studied by quasielastic neutron scattering". United States. https://doi.org/10.1016/J.BBRC.2015.02.134.
@article{osti_22461997,
title = {Internal dynamics of F-actin and myosin subfragment-1 studied by quasielastic neutron scattering},
author = {Matsuo, Tatsuhito and Arata, Toshiaki and Oda, Toshiro and Nakajima, Kenji and Ohira-Kawamura, Seiko and Kikuchi, Tatsuya and Fujiwara, Satoru},
abstractNote = {Various biological functions related to cell motility are driven by the interaction between the partner proteins, actin and myosin. To obtain insights into how this interaction occurs, the internal dynamics of F-actin and myosin subfragment-1 (S1) were characterized by the quasielastic neutron scattering measurements on the solution samples of F-actin and S1. Contributions of the internal motions of the proteins to the scattering spectra were separated from those of the global macromolecular diffusion. Analysis of the spectra arising from the internal dynamics showed that the correlation times of the atomic motions were about two times shorter for F-actin than for S1, suggesting that F-actin fluctuates more rapidly than S1. It was also shown that the fraction of the immobile atoms is larger for S1 than for F-actin. These results suggest that F-actin actively facilitates the binding of myosin by utilizing the more frequent conformational fluctuations than those of S1. - Highlights: • We studied the internal dynamics of F-actin and myosin S1 by neutron scattering. • The correlation times of the atomic motions were smaller for F-actin than for S1. • The fraction of the immobile atoms was also smaller for F-actin than for S1. • Our results suggest that mobility of atoms in F-actin is higher than that in S1. • We propose that high flexibility of F-actin facilitates the binding of myosin.},
doi = {10.1016/J.BBRC.2015.02.134},
url = {https://www.osti.gov/biblio/22461997},
journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 3,
volume = 459,
place = {United States},
year = {Fri Apr 10 00:00:00 EDT 2015},
month = {Fri Apr 10 00:00:00 EDT 2015}
}