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Nanosurgical Manipulation of Titin and Its M-Complex
- Titin is a multifunctional filamentous protein anchored in the M-band, a hexagonally organized supramolecular lattice in the middle of the muscle sarcomere. Functionally, the M-band is a framework that cross-links myosin thick filaments, organizes associated proteins, and maintains sarcomeric symmetry via its structural and putative mechanical properties. Part of the M-band appears at the C-terminal end of isolated titin molecules in the form of a globular head, named here the “M-complex”, which also serves as the point of head-to-head attachment of titin. We used high-resolution atomic force microscopy and nanosurgical manipulation to investigate the topographical and internal structure and local mechanical properties of the M-complex and its associated titin molecules. We find that the M-complex is a stable structure that corresponds to the transverse unit of the M-band organized around the myosin thick filament. M-complexes may be interlinked into an M-complex array that reflects the local structural and mechanical status of the transversal M-band lattice. Local segments of titin and the M-complex could be nanosurgically manipulated to achieve extension and domain unfolding. Long threads could be pulled out of the M-complex, suggesting that it is a compact supramolecular reservoir of extensible filaments. Nanosurgery evoked an unexpected volume increment in the M-complex, which may be related to its function as a mechanical spacer. The M-complex thus displays both elastic and plastic properties which support the idea that the M-band may be involved in mechanical functions within the muscle sarcomere.
Author: | Dominik Sziklai, Judit Sallai, Zsombor Papp, Dalma Kellermayer, Zsolt Mártonfalvi, Ricardo H. Pires, Miklós S. Z. Kellermayer |
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URN: | urn:nbn:de:gbv:9-opus-59375 |
DOI: | https://doi.org/10.3390/nano12020178 |
ISSN: | 2079-4991 |
Parent Title (English): | Nanomaterials |
Publisher: | MDPI |
Place of publication: | Basel |
Editor: | Gabriel Žoldák |
Document Type: | Article |
Language: | English |
Date of first Publication: | 2022/01/06 |
Release Date: | 2022/07/05 |
Tag: | atomic force microscopy; domain unfolding; mechanical stability; molecular mechanics; nanomanipulation; polymer extension; titin |
GND Keyword: | - |
Volume: | 12 |
Article Number: | 178 |
Page Number: | 17 |
Faculties: | Universitätsmedizin |
Licence (German): | Creative Commons - Namensnennung |