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Masui, Tomomi; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Shikinaka, Kazuhiro*; Kwon, H.*; Kakugo, Akira*; Gong, J.*
no journal, ,
no abstracts in English
Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*
no journal, ,
no abstracts in English
Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*
no journal, ,
no abstracts in English
Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*
no journal, ,
Actin is one of the most abundant cytoskeleton proteins in eucaryotic cell. They play a crucialrole in cell motility by polymerizing monomeric globular G-actin into polymeric filamentous actin (F-actin). With actin-binding proteins (ABPs), they form higher order structures such as linear bundles, two-dimensional networks and three-dimensional gels. It has been considered that these structures are controlled by ABPs. However recent study have shown that the only one kind of artificial cationic polymer can form variety of structures depending its concentration and salt concentration. This system is a good model to elucidate the mechanism of regulation of actin and ABPs complex structure. Based on these backgrounds, we have investigated the effects of salt concentration on the stability and structure of actin-polycation complexes by using small angle neutron scattering (SANS) technique.
Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*
no journal, ,
no abstracts in English
Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*
no journal, ,
Actin is one of the cytoskeleton proteins and it is most abundant proteins in eucaryotic cell. They play a crucial role in cell motility by polymerization of monomeric globular G-actin into polymeric filamentous actin (F-actin). With actin binding proteins, they form various structures such as linear bundles, two-dimensional networks, and three-dimensional gels. It has been considered that these structures are controlled by the specific interaction between actin and binding protein. However from the physicochemical point of view, actin has negative charge and actin-binding protein has positive charge. Thus, the electrostatic interaction might play important role to determinein the structure. Based on this idea, we have investigated the effects of salt concentration on the stability and structure of actin-polymer complexes by using small angle neutron scattering (SANS) technique.
Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*
no journal, ,
Actin is one of the cytoskeleton proteins and it is most abundant proteins in eucaryotic cell. They play a crucial role in cell motility by polymerization of monomeric globular G-actin into polymeric filamentous actin (F-actin). With actin binding proteins, they form various structures such as linear bundles, two-dimensional networks, and three-dimensional gels. It has been considered that these structures are controlled by the specific interaction between actin and binding protein. However from the physicochemical point of view, actin has negative charge and actin-binding protein has positive charge. Thus, the electrostatic interaction might play important role to determine in the structure. Based on this idea, we have investigated the effects of salt concentration on the stability and structure of actin-polymer complexes by using small angle neutron scattering (SANS) technique.
Masui, Tomomi; Shikinaka, Kazuhiro*; Kwon, H.*; Koizumi, Satoshi; Hashimoto, Takeji; Iwase, Hiroki; Kakugo, Akira*; Gong, J.*
no journal, ,
Actin is one of the most abundant cytoskeleton proteins in eucaryotic cell. They play a crucial role in cell motility by polymerizing monomeric globular G-actin into polymeric filamentous actin (F-actin). Withactin-binding proteins (ABPs), they form higher order structures such as linear bundles, two-dimensional networks and three-dimensional gels. In this study we have constructed model cytoskeleton system composed of F-actin, cationic polymer and salt. To investigate salt induced hierarchical structure change we employed fluorescence microscopy and small angle neutron scattering (SANS) technique.
Masui, Tomomi; Shikinaka, Kazuhiro*; Koizumi, Satoshi; Hashimoto, Takeji; Kakugo, Akira*; Gong, J.*; Kwon, H.*
no journal, ,
We reconstituted in vitro model cytoskeleton using F-actin and polycation. We have investigated hierarchical structural change of F-actin/polycation complexes induced by salt quantitatively by fluorescence microscopy and small angle neutron scattering. Based on the obtained structural parameters, we will discuss dominant interactions which determine the structure.
Masui, Tomomi; Shikinaka, Kazuhiro*; Koizumi, Satoshi; Kakugo, Akira*; Hashimoto, Takeji; Gong, J.*
no journal, ,
Hierarchical structures of F-actin, an anionic polyelectrolyte, and PDMAPAA-Q, a synthetic linear cationic polyelectrolyte (polycation), complexes in KCl salt solutions have been examined over a wide range of length scales from nanometer to micrometer using a combination of ultra-small-angle neutron scattering technique and fluorescence microscopy. We found hierarchical condensation of actin/polycation complex composed of a superbundle of 10 micrometer, protobundle of 100 nanometer, and protofilament (F-actin) of nanometer. These structures are largely influenced by salt concentrations. With increase of salt concentration superbundle structure changes from globular to extended states, simultaneously, the regularity of F-actin inside the protobundle increased and protobundle size increased about ten times larger. Further increase of salt concentration brings the protobundle disassemble to single F-actin.