Slowly modulating fluctuations as mesoscopic distortions occurring on an actin filament
An actin filament sliding on myosin molecules exhibits fluctuating or staggered movements as responding to changes in the ATP concentration. We previously observed that fluctuations in the sliding velocity enhanced in a manner being independent of the magnitude of the velocity. The present study foc...
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| Veröffentlicht in: | BioSystems 2009-04, Vol.96 (1), p.14-18 |
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| creator | Hatori, Kuniyuki Matsui, Masahiro Omote, Yoichiro |
| description | An actin filament sliding on myosin molecules exhibits fluctuating or staggered movements as responding to changes in the ATP concentration. We previously observed that fluctuations in the sliding velocity enhanced in a manner being independent of the magnitude of the velocity. The present study focused upon a single actin filament bound to a glass surface through avidin–biotin bonding to examine those fluctuations inherent to the filament in the presence of heavy meromyosin. The auto-correlation analysis revealed that the relaxation time of fluctuations in the filamental displacement obtains its maximum value at about 100
μM of the ATP concentration in the ambient, while the magnitude of the fluctuations gradually increased with an increase of the concentration. Furthermore, the measurement of the fluorescence intensity from the markers fixed on the filament demonstrated an enhancement of the negative correlation between the measured peak intensity and the spatial spreading of its intensity over the range of 0–200
μM of the ATP concentration, as indicating both development and mitigation of local distortions occurring within the filament. |
| doi_str_mv | 10.1016/j.biosystems.2008.11.003 |
| format | Article |
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μM of the ATP concentration in the ambient, while the magnitude of the fluctuations gradually increased with an increase of the concentration. Furthermore, the measurement of the fluorescence intensity from the markers fixed on the filament demonstrated an enhancement of the negative correlation between the measured peak intensity and the spatial spreading of its intensity over the range of 0–200
μM of the ATP concentration, as indicating both development and mitigation of local distortions occurring within the filament.</description><subject>Actin Cytoskeleton - chemistry</subject><subject>Actin Cytoskeleton - ultrastructure</subject><subject>Actin filament</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>ATP-dependence</subject><subject>Computer Simulation</subject><subject>Fluctuations</subject><subject>Models, Chemical</subject><subject>Models, Molecular</subject><subject>Molecular Motor Proteins - chemistry</subject><subject>Molecular Motor Proteins - ultrastructure</subject><subject>Motion</subject><subject>Myosin</subject><subject>Myosins - chemistry</subject><subject>Myosins - ultrastructure</subject><subject>Protein Conformation</subject><subject>Sliding movement</subject><subject>Structural change</subject><issn>0303-2647</issn><issn>1872-8324</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1r3EAMhofS0GzS_oXiU2925sue8bENzQcs5JCEHIexLJdZbM92ZLfsv-8su5BjhUACva-EHsYKwSvBRXOzq7oQ6UALTlRJzm0lRMW5-sA2whpZWiX1R7bhiqtSNtpcsiuiHc9RW_GJXYqW163iesPensf4dzwUU-zX0S9h_lUM4wrLmvs4U-GpmJAiQdwHKPpAS0ynSQRYUzoa4lz4nJDdxRBGP-G8fGYXgx8Jv5zrNXu9-_ly-1Bun-4fb79vS9DKLiVIj731XQ-DkVDbQRrbeW2VNkq1VrZt4w1ajdBY23Zq6EzT6rrzymrwnVLX7Ntp7z7F3yvS4qZAgOPoZ4wrucZwLuvWZKE9CSFFooSD26cw-XRwgrsjVLdz71DdEaoTwmWo2fr1fGPtJuzfjWeKWfDjJMD86Z-AyREEnAH7kBAW18fw_yv_AKaqkFw</recordid><startdate>20090401</startdate><enddate>20090401</enddate><creator>Hatori, Kuniyuki</creator><creator>Matsui, Masahiro</creator><creator>Omote, Yoichiro</creator><general>Elsevier Ireland Ltd</general><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></search><sort><creationdate>20090401</creationdate><title>Slowly modulating fluctuations as mesoscopic distortions occurring on an actin filament</title><author>Hatori, Kuniyuki ; Matsui, Masahiro ; Omote, Yoichiro</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c438t-c2aed8abdcf72c58f278ba4834733982996a7e84ec6889b3fb76945ba384cab33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Actin Cytoskeleton - chemistry</topic><topic>Actin Cytoskeleton - ultrastructure</topic><topic>Actin filament</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>ATP-dependence</topic><topic>Computer Simulation</topic><topic>Fluctuations</topic><topic>Models, Chemical</topic><topic>Models, Molecular</topic><topic>Molecular Motor Proteins - chemistry</topic><topic>Molecular Motor Proteins - ultrastructure</topic><topic>Motion</topic><topic>Myosin</topic><topic>Myosins - chemistry</topic><topic>Myosins - ultrastructure</topic><topic>Protein Conformation</topic><topic>Sliding movement</topic><topic>Structural change</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hatori, Kuniyuki</creatorcontrib><creatorcontrib>Matsui, Masahiro</creatorcontrib><creatorcontrib>Omote, Yoichiro</creatorcontrib><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><jtitle>BioSystems</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hatori, Kuniyuki</au><au>Matsui, Masahiro</au><au>Omote, Yoichiro</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Slowly modulating fluctuations as mesoscopic distortions occurring on an actin filament</atitle><jtitle>BioSystems</jtitle><addtitle>Biosystems</addtitle><date>2009-04-01</date><risdate>2009</risdate><volume>96</volume><issue>1</issue><spage>14</spage><epage>18</epage><pages>14-18</pages><issn>0303-2647</issn><eissn>1872-8324</eissn><abstract>An actin filament sliding on myosin molecules exhibits fluctuating or staggered movements as responding to changes in the ATP concentration. We previously observed that fluctuations in the sliding velocity enhanced in a manner being independent of the magnitude of the velocity. The present study focused upon a single actin filament bound to a glass surface through avidin–biotin bonding to examine those fluctuations inherent to the filament in the presence of heavy meromyosin. The auto-correlation analysis revealed that the relaxation time of fluctuations in the filamental displacement obtains its maximum value at about 100
μM of the ATP concentration in the ambient, while the magnitude of the fluctuations gradually increased with an increase of the concentration. Furthermore, the measurement of the fluorescence intensity from the markers fixed on the filament demonstrated an enhancement of the negative correlation between the measured peak intensity and the spatial spreading of its intensity over the range of 0–200
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| fulltext | fulltext |
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| ispartof | BioSystems, 2009-04, Vol.96 (1), p.14-18 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Actin Cytoskeleton - chemistry Actin Cytoskeleton - ultrastructure Actin filament Adenosine Triphosphate - chemistry ATP-dependence Computer Simulation Fluctuations Models, Chemical Models, Molecular Molecular Motor Proteins - chemistry Molecular Motor Proteins - ultrastructure Motion Myosin Myosins - chemistry Myosins - ultrastructure Protein Conformation Sliding movement Structural change |
| title | Slowly modulating fluctuations as mesoscopic distortions occurring on an actin filament |
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