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dc.contributor.authorTanaka, Hiroto
dc.contributor.authorHomma, Kazuaki
dc.contributor.authorIwane, Atsuko Hikikoshi
dc.contributor.authorKatayama, Eisaku
dc.contributor.authorIkebe, Reiko
dc.contributor.authorSaito, Junya
dc.contributor.authorYanagida, Toshio
dc.contributor.authorIkebe, Mitsuo
dc.date2022-08-11T08:08:49.000
dc.date.accessioned2022-08-23T16:09:19Z
dc.date.available2022-08-23T16:09:19Z
dc.date.issued2002-01-24
dc.date.submitted2009-01-13
dc.identifier.citationNature. 2002 Jan 10;415(6868):192-5. <a href="http://dx.doi.org/10.1038/415192a">Link to article on publisher's site</a>
dc.identifier.issn0028-0836 (Print)
dc.identifier.doi10.1038/415192a
dc.identifier.pmid11805840
dc.identifier.urihttp://hdl.handle.net/20.500.14038/32666
dc.description.abstractClass-V myosin proceeds along actin filaments with large ( approximately 36 nm) steps. Myosin-V has two heads, each of which consists of a motor domain and a long (23 nm) neck domain. In accordance with the widely accepted lever-arm model, it was suggested that myosin-V steps to successive (36 nm) target zones along the actin helical repeat by tilting its long neck (lever-arm). To test this hypothesis, we measured the mechanical properties of single molecules of myosin-V truncation mutants with neck domains only one-sixth of the native length. Our results show that the processivity and step distance along actin are both similar to those of full-length myosin-V. Thus, the long neck domain is not essential for either the large steps or processivity of myosin-V. These results challenge the lever-arm model. We propose that the motor domain and/or the actomyosin interface enable myosin-V to produce large processive steps during translocation along actin.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=11805840&dopt=Abstract">Link to Article in PubMed</a>
dc.relation.urlhttp://dx.doi.org/10.1038/415192a
dc.subjectActins; Adenosine Triphosphate; Animals; Biomechanics; Chickens; Escherichia coli; Models, Biological; Molecular Motor Proteins; Mutation; Myosin Type V; Protein Structure, Tertiary; Recombinant Fusion Proteins; Xenopus
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleThe motor domain determines the large step of myosin-V
dc.typeJournal Article
dc.source.journaltitleNature
dc.source.volume415
dc.source.issue6868
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/1226
dc.identifier.contextkey693136
html.description.abstract<p>Class-V myosin proceeds along actin filaments with large ( approximately 36 nm) steps. Myosin-V has two heads, each of which consists of a motor domain and a long (23 nm) neck domain. In accordance with the widely accepted lever-arm model, it was suggested that myosin-V steps to successive (36 nm) target zones along the actin helical repeat by tilting its long neck (lever-arm). To test this hypothesis, we measured the mechanical properties of single molecules of myosin-V truncation mutants with neck domains only one-sixth of the native length. Our results show that the processivity and step distance along actin are both similar to those of full-length myosin-V. Thus, the long neck domain is not essential for either the large steps or processivity of myosin-V. These results challenge the lever-arm model. We propose that the motor domain and/or the actomyosin interface enable myosin-V to produce large processive steps during translocation along actin.</p>
dc.identifier.submissionpathgsbs_sp/1226
dc.contributor.departmentDepartment of Physiology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages192-5


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