Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin
Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin bindin...
Ausführliche Beschreibung
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| Autor*in: |
Shchepkin, Daniil V. [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2017 |
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| Schlagwörter: |
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| Anmerkung: |
© Springer International Publishing Switzerland 2017 |
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| Übergeordnetes Werk: |
Enthalten in: Journal of muscle research and cell motility - Springer International Publishing, 1980, 38(2017), 2 vom: Apr., Seite 183-191 |
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| Übergeordnetes Werk: |
volume:38 ; year:2017 ; number:2 ; month:04 ; pages:183-191 |
| Links: |
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| DOI / URN: |
10.1007/s10974-017-9472-x |
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| Katalog-ID: |
OLC2067130889 |
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| 245 | 1 | 0 | |a Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin |
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| 520 | |a Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. | ||
| 650 | 4 | |a Regulation of muscle contraction | |
| 650 | 4 | |a Tropomyosin | |
| 650 | 4 | |a Actin | |
| 650 | 4 | |a Myosin | |
| 650 | 4 | |a motility assay | |
| 650 | 4 | |a Optical trap | |
| 700 | 1 | |a Nabiev, Salavat R. |4 aut | |
| 700 | 1 | |a Kopylova, Galina V. |4 aut | |
| 700 | 1 | |a Matyushenko, Alexander M. |4 aut | |
| 700 | 1 | |a Levitsky, Dmitrii I. |4 aut | |
| 700 | 1 | |a Bershitsky, Sergey Y. |4 aut | |
| 700 | 1 | |a Tsaturyan, Andrey K. |4 aut | |
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10.1007/s10974-017-9472-x doi (DE-627)OLC2067130889 (DE-He213)s10974-017-9472-x-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Shchepkin, Daniil V. verfasserin aut Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer International Publishing Switzerland 2017 Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. Regulation of muscle contraction Tropomyosin Actin Myosin motility assay Optical trap Nabiev, Salavat R. aut Kopylova, Galina V. aut Matyushenko, Alexander M. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Tsaturyan, Andrey K. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 38(2017), 2 vom: Apr., Seite 183-191 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:38 year:2017 number:2 month:04 pages:183-191 https://doi.org/10.1007/s10974-017-9472-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4219 AR 38 2017 2 04 183-191 |
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10.1007/s10974-017-9472-x doi (DE-627)OLC2067130889 (DE-He213)s10974-017-9472-x-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Shchepkin, Daniil V. verfasserin aut Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer International Publishing Switzerland 2017 Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. Regulation of muscle contraction Tropomyosin Actin Myosin motility assay Optical trap Nabiev, Salavat R. aut Kopylova, Galina V. aut Matyushenko, Alexander M. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Tsaturyan, Andrey K. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 38(2017), 2 vom: Apr., Seite 183-191 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:38 year:2017 number:2 month:04 pages:183-191 https://doi.org/10.1007/s10974-017-9472-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4219 AR 38 2017 2 04 183-191 |
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10.1007/s10974-017-9472-x doi (DE-627)OLC2067130889 (DE-He213)s10974-017-9472-x-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Shchepkin, Daniil V. verfasserin aut Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer International Publishing Switzerland 2017 Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. Regulation of muscle contraction Tropomyosin Actin Myosin motility assay Optical trap Nabiev, Salavat R. aut Kopylova, Galina V. aut Matyushenko, Alexander M. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Tsaturyan, Andrey K. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 38(2017), 2 vom: Apr., Seite 183-191 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:38 year:2017 number:2 month:04 pages:183-191 https://doi.org/10.1007/s10974-017-9472-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4219 AR 38 2017 2 04 183-191 |
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10.1007/s10974-017-9472-x doi (DE-627)OLC2067130889 (DE-He213)s10974-017-9472-x-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Shchepkin, Daniil V. verfasserin aut Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer International Publishing Switzerland 2017 Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. Regulation of muscle contraction Tropomyosin Actin Myosin motility assay Optical trap Nabiev, Salavat R. aut Kopylova, Galina V. aut Matyushenko, Alexander M. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Tsaturyan, Andrey K. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 38(2017), 2 vom: Apr., Seite 183-191 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:38 year:2017 number:2 month:04 pages:183-191 https://doi.org/10.1007/s10974-017-9472-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4219 AR 38 2017 2 04 183-191 |
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10.1007/s10974-017-9472-x doi (DE-627)OLC2067130889 (DE-He213)s10974-017-9472-x-p DE-627 ger DE-627 rakwb eng 590 570 VZ 12 ssgn BIODIV DE-30 fid Shchepkin, Daniil V. verfasserin aut Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin 2017 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier © Springer International Publishing Switzerland 2017 Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. Regulation of muscle contraction Tropomyosin Actin Myosin motility assay Optical trap Nabiev, Salavat R. aut Kopylova, Galina V. aut Matyushenko, Alexander M. aut Levitsky, Dmitrii I. aut Bershitsky, Sergey Y. aut Tsaturyan, Andrey K. aut Enthalten in Journal of muscle research and cell motility Springer International Publishing, 1980 38(2017), 2 vom: Apr., Seite 183-191 (DE-627)166717754 (DE-600)283053-X (DE-576)015170152 0142-4319 nnns volume:38 year:2017 number:2 month:04 pages:183-191 https://doi.org/10.1007/s10974-017-9472-x lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_OLC FID-BIODIV SSG-OLC-WIW GBV_ILN_2221 GBV_ILN_4012 GBV_ILN_4219 AR 38 2017 2 04 183-191 |
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Enthalten in Journal of muscle research and cell motility 38(2017), 2 vom: Apr., Seite 183-191 volume:38 year:2017 number:2 month:04 pages:183-191 |
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Shchepkin, Daniil V. @@aut@@ Nabiev, Salavat R. @@aut@@ Kopylova, Galina V. @@aut@@ Matyushenko, Alexander M. @@aut@@ Levitsky, Dmitrii I. @@aut@@ Bershitsky, Sergey Y. @@aut@@ Tsaturyan, Andrey K. @@aut@@ |
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Shchepkin, Daniil V. Nabiev, Salavat R. Kopylova, Galina V. Matyushenko, Alexander M. Levitsky, Dmitrii I. Bershitsky, Sergey Y. Tsaturyan, Andrey K. |
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cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin |
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Cooperativity of myosin interaction with thin filaments is enhanced by stabilizing substitutions in tropomyosin |
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Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. © Springer International Publishing Switzerland 2017 |
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Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. © Springer International Publishing Switzerland 2017 |
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Abstract Muscle contraction is powered by myosin interaction with actin-based thin filaments containing $ Ca^{2+} $-regulatory proteins, tropomyosin and troponin. Coiled-coil tropomyosin molecules form a long helical strand that winds around actin filament and either shields actin from myosin binding or opens it. Non-canonical residues G126 and D137 in the central part of tropomyosin destabilize its coiled-coil structure. Their substitutions for canonical ones, G126R and D137L, increase structural stability and the velocity of sliding of reconstructed thin filaments along myosin coated surface. The effect of these stabilizing mutations on force of the actin–myosin interaction is unknown. It also remains unclear whether the stabilization affects single actin–myosin interactions or it modifies the cooperativity of the binding of myosin molecules to actin. We used an optical trap to measure the effects of the stabilization on step size, unitary force and duration of the interactions at low and high load and compared the results with those obtained in an in vitro motility assay. We found that significant prolongation of lifetime of the actin–myosin complex under high load observed at high extent of tropomyosin stabilization, i.e. with double mutant, G126R/D137L, correlates with higher force in the motility assay. Also, the higher the extent of stabilization of tropomyosin, the fewer myosin molecules are needed to propel the thin filaments. The data suggest that the effects of the stabilizing mutations in tropomyosin on the myosin interaction with regulated thin filaments are mainly realized via cooperative mechanisms by increasing the size of cooperative unit. © Springer International Publishing Switzerland 2017 |
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