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Journal Article

Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes.

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Lenart,  P.
Research Group of Cytoskeletal Dynamics in Oocytes, MPI for Biophysical Chemistry, Max Planck Society;

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3181824.pdf
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3181824-Suppl.pdf
(Supplementary material), 2MB

3181824-Suppl-2.pdf
(Supplementary material), 16MB

Citation

Szikora, S., Gajdos, T., Novák, T., Farkas, D., Földi, I., Lenart, P., et al. (2020). Nanoscopy reveals the layered organization of the sarcomeric H-zone and I-band complexes. Journal of Cell Biology, 219(1): e201907026. doi:10.1083/jcb.201907026.


Cite as: https://hdl.handle.net/21.11116/0000-0005-5911-4
Abstract
Sarcomeres are extremely highly ordered macromolecular assemblies where structural organization is intimately linked to their functionality as contractile units. Although the structural basis of actin and Myosin interaction is revealed at a quasiatomic resolution, much less is known about the molecular organization of the I-band and H-zone. We report the development of a powerful nanoscopic approach, combined with a structure-averaging algorithm, that allowed us to determine the position of 27 sarcomeric proteins in Drosophila melanogaster flight muscles with a quasimolecular, ∼5- to 10-nm localization precision. With this protein localization atlas and template-based protein structure modeling, we have assembled refined I-band and H-zone models with unparalleled scope and resolution. In addition, we found that actin regulatory proteins of the H-zone are organized into two distinct layers, suggesting that the major place of thin filament assembly is an M-line-centered narrow domain where short actin oligomers can form and subsequently anneal to the pointed end.