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Dynamic assembly properties of nonmuscle myosin II isoforms revealed by combination of fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy

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Title: Dynamic assembly properties of nonmuscle myosin II isoforms revealed by combination of fluorescence correlation spectroscopy and fluorescence cross-correlation spectroscopy
Authors: Mitsuhashi, Mariko Browse this author
Sakata, Hiroshi Browse this author
Kinjo, Masataka Browse this author
Yazawa, Michio Browse this author
Takahashi, Masayuki Browse this author →KAKEN DB
Keywords: assembly
FCCS
myosin II
FCS
Mts1 (S100A4)
Issue Date: Mar-2011
Publisher: Oxford University Press
Journal Title: The Journal of Biochemistry
Volume: 149
Issue: 3
Start Page: 253
End Page: 263
Publisher DOI: 10.1093/jb/mvq134
PMID: 21106542
Abstract: Myosin II molecules assemble into filaments through their C-terminal rod region, and are responsible for several cellular motile activities. Three isoforms of nonmuscle myosin II (IIA, IIB and IIC) are expressed in mammalian cells. However, little is known regarding the isoform composition in filaments. To obtain new insight into the assembly properties of myosin II isoforms, especially regarding the isoform composition in filaments, we performed a combination analysis of fluorescence correlation spectroscopy (FCS) and fluorescence cross-correlation spectroscopy (FCCS), which enables us to acquire information on both the interaction and the size of each molecule simultaneously. Using C-terminal rod fragments of IIA and IIB (ARF296 and BRF305) labelled with different fluorescent probes, we demonstrated that hetero-assemblies were formed from a mixture of ARF296 and BRF305, and that dynamic exchange of rod fragments occurred between pre-formed homo-assemblies of each isoform in an isoform-independent manner. We also showed that Mts1 (S100A4) specifically stripped ARF296 away from the hetero-assemblies, and consequently, homo-assemblies of BRF305 were formed. These results suggest that IIA and IIB can form hetero-filaments in an isoform-independent manner, and that a factor like Mts1 can remove one isoform from the hetero-filament, resulting in a formation of homo-filaments consisting of another isoform.
Rights: This is a pre-copy-editing, author-produced PDF of an article accepted for publication in The Journal of Biochemistry following peer review. The definitive publisher-authenticated version, J Biochem (2011) 149 (3): 253-263, is available online at: http://jb.oxfordjournals.org/content/149/3/253
Type: article (author version)
URI: http://hdl.handle.net/2115/47493
Appears in Collections:理学院・理学研究院 (Graduate School of Science / Faculty of Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 高橋 正行

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