Cooperative Regulation of Myosin-Actin Interactions by a Continuous Flexible Chain I: Actin-Tropomyosin Systems
We present a model for cooperative myosin binding to the regulated actin filament, where tropomyosins are treated as a weakly-confined continuous flexible chain covering myosin binding sites. Thermal fluctuations in chain orientation are initially required for myosin binding, leaving kinked regions...
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| Veröffentlicht in: | Biophysical journal 2003-05, Vol.84 (5), p.3155-3167 |
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| creator | Smith, D.A. Maytum, R. Geeves, M.A. |
| description | We present a model for cooperative myosin binding to the regulated actin filament, where tropomyosins are treated as a weakly-confined continuous flexible chain covering myosin binding sites. Thermal fluctuations in chain orientation are initially required for myosin binding, leaving kinked regions under which subsequent myosins may bind without further distortion of the chain. Statistical mechanics predicts the fraction of sites with bound myosin-S1 as a function of their affinities. Published S1 binding curves to regulated filaments with different tropomyosin isoforms are fitted by varying the binding constant, chain persistence length ν (in actin monomers), and chain kink energy A from a single bound S1. With skeletal tropomyosin, we find an S1 actin-binding constant of 2.2×107M−1, A=1.6 kBT and ν=2.7. Similar persistence lengths are found with yeast tropomyosin. Larger values are found for tropomyosin-troponin in the presence of calcium (ν=3.7) and tropomyosins from smooth muscle and fibroblasts (ν=4.5). The relationship of these results to structural information and the rigid-unit model of McKillop and Geeves is discussed. |
| doi_str_mv | 10.1016/S0006-3495(03)70040-X |
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Thermal fluctuations in chain orientation are initially required for myosin binding, leaving kinked regions under which subsequent myosins may bind without further distortion of the chain. Statistical mechanics predicts the fraction of sites with bound myosin-S1 as a function of their affinities. Published S1 binding curves to regulated filaments with different tropomyosin isoforms are fitted by varying the binding constant, chain persistence length ν (in actin monomers), and chain kink energy A from a single bound S1. With skeletal tropomyosin, we find an S1 actin-binding constant of 2.2×107M−1, A=1.6 kBT and ν=2.7. Similar persistence lengths are found with yeast tropomyosin. Larger values are found for tropomyosin-troponin in the presence of calcium (ν=3.7) and tropomyosins from smooth muscle and fibroblasts (ν=4.5). 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Thermal fluctuations in chain orientation are initially required for myosin binding, leaving kinked regions under which subsequent myosins may bind without further distortion of the chain. Statistical mechanics predicts the fraction of sites with bound myosin-S1 as a function of their affinities. Published S1 binding curves to regulated filaments with different tropomyosin isoforms are fitted by varying the binding constant, chain persistence length ν (in actin monomers), and chain kink energy A from a single bound S1. With skeletal tropomyosin, we find an S1 actin-binding constant of 2.2×107M−1, A=1.6 kBT and ν=2.7. Similar persistence lengths are found with yeast tropomyosin. Larger values are found for tropomyosin-troponin in the presence of calcium (ν=3.7) and tropomyosins from smooth muscle and fibroblasts (ν=4.5). The relationship of these results to structural information and the rigid-unit model of McKillop and Geeves is discussed.</description><subject>Actins - chemistry</subject><subject>Actins - physiology</subject><subject>Binding Sites</subject><subject>Computer Simulation</subject><subject>Feedback</subject><subject>Homeostasis</subject><subject>Macromolecular Substances</subject><subject>Models, Biological</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Motor Proteins - chemistry</subject><subject>Molecular Motor Proteins - physiology</subject><subject>Motion</subject><subject>Muscle Contraction - physiology</subject><subject>Muscles and Contractility</subject><subject>Myosins - chemistry</subject><subject>Myosins - physiology</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Tropomyosin - chemistry</subject><subject>Tropomyosin - physiology</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUtv1DAUhS0EokPhJ4C8QmURev1KJiyoqohCpSIkWqTuLMe5bo2SeLCTEfPv8TxUYNWVLZ3vnHvtQ8hrBu8ZsPL0GgDKQshanYB4VwFIKG6fkAVTkhcAy_IpWTwgR-RFSj8BGFfAnpMjxitWc6kWJDQhrDCaya-Rfse7uc_XMNLg6NdNSH4szu3kR3o5TpmyWy3RdkMNbcKYhTnMiV70-Nu3PdLm3mzZD3RnKm5iWIVhF0OvN2nCIb0kz5zpE746nMfkx8Wnm-ZLcfXt82VzflVYWYqpYFxC5WrjSnSurkzXcYmdcqa0bdu1TKKzYFhdCiE7QClZ3XKORilVMVspcUw-7nNXcztgZ3Gcoun1KvrBxI0Oxuv_ldHf67uw1kwAX1ZlDnh7CIjh14xp0oNPFvvejJjfrCvBZVkveQbVHrQxpBTRPQxhoLdV6V1VetuDBqF3Venb7Hvz74Z_XYduMnC2BzD_09pj1Ml6HC12PqKddBf8IyP-AA80pwU</recordid><startdate>200305</startdate><enddate>200305</enddate><creator>Smith, D.A.</creator><creator>Maytum, R.</creator><creator>Geeves, M.A.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>200305</creationdate><title>Cooperative Regulation of Myosin-Actin Interactions by a Continuous Flexible Chain I: Actin-Tropomyosin Systems</title><author>Smith, D.A. ; Maytum, R. ; Geeves, M.A.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c463t-12407f9af6eff97add24ed5fa6cbbdb14efc0a196334d0e4419b22ea55571c753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Actins - chemistry</topic><topic>Actins - physiology</topic><topic>Binding Sites</topic><topic>Computer Simulation</topic><topic>Feedback</topic><topic>Homeostasis</topic><topic>Macromolecular Substances</topic><topic>Models, Biological</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Motor Proteins - chemistry</topic><topic>Molecular Motor Proteins - physiology</topic><topic>Motion</topic><topic>Muscle Contraction - physiology</topic><topic>Muscles and Contractility</topic><topic>Myosins - chemistry</topic><topic>Myosins - physiology</topic><topic>Protein Binding</topic><topic>Protein Conformation</topic><topic>Tropomyosin - chemistry</topic><topic>Tropomyosin - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smith, D.A.</creatorcontrib><creatorcontrib>Maytum, R.</creatorcontrib><creatorcontrib>Geeves, M.A.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smith, D.A.</au><au>Maytum, R.</au><au>Geeves, M.A.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cooperative Regulation of Myosin-Actin Interactions by a Continuous Flexible Chain I: Actin-Tropomyosin Systems</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>2003-05</date><risdate>2003</risdate><volume>84</volume><issue>5</issue><spage>3155</spage><epage>3167</epage><pages>3155-3167</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><abstract>We present a model for cooperative myosin binding to the regulated actin filament, where tropomyosins are treated as a weakly-confined continuous flexible chain covering myosin binding sites. Thermal fluctuations in chain orientation are initially required for myosin binding, leaving kinked regions under which subsequent myosins may bind without further distortion of the chain. Statistical mechanics predicts the fraction of sites with bound myosin-S1 as a function of their affinities. Published S1 binding curves to regulated filaments with different tropomyosin isoforms are fitted by varying the binding constant, chain persistence length ν (in actin monomers), and chain kink energy A from a single bound S1. With skeletal tropomyosin, we find an S1 actin-binding constant of 2.2×107M−1, A=1.6 kBT and ν=2.7. Similar persistence lengths are found with yeast tropomyosin. Larger values are found for tropomyosin-troponin in the presence of calcium (ν=3.7) and tropomyosins from smooth muscle and fibroblasts (ν=4.5). The relationship of these results to structural information and the rigid-unit model of McKillop and Geeves is discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12719245</pmid><doi>10.1016/S0006-3495(03)70040-X</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Actins - chemistry Actins - physiology Binding Sites Computer Simulation Feedback Homeostasis Macromolecular Substances Models, Biological Models, Chemical Models, Molecular Molecular Motor Proteins - chemistry Molecular Motor Proteins - physiology Motion Muscle Contraction - physiology Muscles and Contractility Myosins - chemistry Myosins - physiology Protein Binding Protein Conformation Tropomyosin - chemistry Tropomyosin - physiology |
| title | Cooperative Regulation of Myosin-Actin Interactions by a Continuous Flexible Chain I: Actin-Tropomyosin Systems |
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