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The cryo-EM 3D image reconstruction of isolated Lethocerus indicus Z-discs.
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- Additional Information
- Source:
Publisher: Springer Netherlands Country of Publication: Netherlands NLM ID: 8006298 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1573-2657 (Electronic) Linking ISSN: 01424319 NLM ISO Abbreviation: J Muscle Res Cell Motil Subsets: MEDLINE
- Publication Information:
Publication: Dordrecht : Springer Netherlands
Original Publication: [London] Chapman and Hall.
- Subject Terms:
- Abstract:
The Z-disk of striated muscle defines the ends of the sarcomere, which repeats many times within the muscle fiber. Here we report application of cryoelectron tomography and subtomogram averaging to Z-disks isolated from the flight muscles of the large waterbug Lethocerus indicus. We use high salt solutions to remove the myosin containing filaments and use gelsolin to remove the actin filaments of the A- and I-bands leaving only the thin filaments within the Z-disk which were then frozen for cryoelectron microscopy. The Lethocerus Z-disk structure is similar in many ways to the previously studied Z-disk of the honeybee Apis mellifera. At the corners of the unit cell are positioned trimers of paired antiparallel F-actins defining a large solvent channel, whereas at the trigonal positions are positioned F-actin trimers converging slowly towards their (+) ends defining a small solvent channel through the Z-disk. These near parallel F-actins terminate at different Z-heights within the Z-disk. The two types of solvent channel in Lethocerus are similar in size compared to those of Apis which are very different in size. Two types of α-actinin crosslinks were observed between oppositely oriented actin filaments. In one of these, the α-actinin long axis is almost parallel to the F-actins it crosslinks. In the other, the α-actinins are at a small but distinctive angle with respect to the crosslinked actin filaments. The utility of isolated Z-disks for structure determination is discussed.
(© 2023. The Author(s), under exclusive licence to Springer Nature Switzerland AG.)
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- Grant Information:
S10 RR025080 United States RR NCRR NIH HHS; S10 OD018142 United States OD NIH HHS; R01 GM30598 United States GM NIGMS NIH HHS; R35 GM139616 United States GM NIGMS NIH HHS; S10 OD018142 United States CD ODCDC CDC HHS; R01 GM030598 United States GM NIGMS NIH HHS; R01 GM30598 United States GM NIGMS NIH HHS; S10 RR025080 United States RR NCRR NIH HHS; S10 OD018142 United States CD ODCDC CDC HHS
- Contributed Indexing:
Keywords: Electron tomography; F-actin; Kettin; Projectin; α-Actinin
- Accession Number:
0 (Actins)
11003-00-2 (Actinin)
0 (Muscle Proteins)
0 (Solvents)
- Publication Date:
Date Created: 20230903 Date Completed: 20231124 Latest Revision: 20241202
- Publication Date:
20241204
- Accession Number:
PMC10843718
- Accession Number:
10.1007/s10974-023-09657-1
- Accession Number:
37661214
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