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dc.contributor.authorBurgoyne, T
dc.contributor.authorHeumann, JM
dc.contributor.authorMorris, EP
dc.contributor.authorKnupp, C
dc.contributor.authorLiu, J
dc.contributor.authorReedy, MK
dc.contributor.authorTaylor, KA
dc.contributor.authorWang, K
dc.contributor.authorLuther, PK
dc.date.accessioned2019-09-30T08:46:38Z
dc.date.issued2019-07-18
dc.identifier.citationProceedings of the National Academy of Sciences of the United States of America, 2019, 116 (31), pp. 15534 - 15539
dc.identifier.issn0027-8424
dc.identifier.urihttps://repository.icr.ac.uk/handle/internal/3369
dc.identifier.eissn1091-6490
dc.identifier.doi10.1073/pnas.1902235116
dc.description.abstractStriated muscle enables movement in all animals by the contraction of myriads of sarcomeres joined end to end by the Z-bands. The contraction is due to tension generated in each sarcomere between overlapping arrays of actin and myosin filaments. At the Z-band, actin filaments from adjoining sarcomeres overlap and are cross-linked in a regular pattern mainly by the protein α-actinin. The Z-band is dynamic, reflected by the 2 regular patterns seen in transverse section electron micrographs; the so-called small-square and basketweave forms. Although these forms are attributed, respectively, to relaxed and actively contracting muscles, the basketweave form occurs in certain relaxed muscles as in the muscle studied here. We used electron tomography and subtomogram averaging to derive the 3D structure of the Z-band in the swimbladder sonic muscle of type I male plainfin midshipman fish ( Porichthys notatus) , into which we docked the crystallographic structures of actin and α-actinin. The α-actinin links run diagonally between connected pairs of antiparallel actin filaments and are oriented at an angle of about 25° away from the actin filament axes. The slightly curved and flattened structure of the α-actinin rod has a distinct fit into the map. The Z-band model provides a detailed understanding of the role of α-actinin in transmitting tension between actin filaments in adjoining sarcomeres.
dc.formatPrint-Electronic
dc.format.extent15534 - 15539
dc.languageeng
dc.language.isoeng
dc.rights.urihttps://www.rioxx.net/licenses/under-embargo-all-rights-reserved
dc.subjectSarcomeres
dc.subjectAir Sacs
dc.subjectAnimals
dc.subjectFishes
dc.subjectActinin
dc.subjectFish Proteins
dc.subjectMuscle Contraction
dc.subjectMale
dc.titleThree-dimensional structure of the basketweave Z-band in midshipman fish sonic muscle.
dc.typeJournal Article
rioxxterms.versionofrecord10.1073/pnas.1902235116
rioxxterms.licenseref.urihttps://www.rioxx.net/licenses/under-embargo-all-rights-reserved
rioxxterms.licenseref.startdate2019-07-18
rioxxterms.typeJournal Article/Review
dc.relation.isPartOfProceedings of the National Academy of Sciences of the United States of America
pubs.issue31
pubs.notesNo embargo
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy
pubs.organisational-group/ICR
pubs.organisational-group/ICR/Primary Group
pubs.organisational-group/ICR/Primary Group/ICR Divisions
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology
pubs.organisational-group/ICR/Primary Group/ICR Divisions/Structural Biology/Structural Electron Microscopy
pubs.publication-statusPublished
pubs.volume116
pubs.embargo.termsNo embargo
icr.researchteamStructural Electron Microscopyen_US
dc.contributor.icrauthorMorris, Edwarden


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