ArticleProceedings of the National Academy of Sciences of the United States of America2006
The molecular elasticity of the insect flight muscle proteins projectin and kettin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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36 citing papers in PubMed, 91 citations in OpenAlex.
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- Rolling Adhesion of Schizont Stage Malaria-Infected Red Blood Cells in Shear Flow.Biophysical journal · 2017Article
- Structure of myosin filaments from relaxedScience advances · 2016Article
- Elastic proteins in the flight muscle of Manduca sexta.Archives of biochemistry and biophysics · 2015Article
- The nebulin repeat protein Lasp regulates I-band architecture and filament spacing in myofibrils.The Journal of cell biology · 2014Article
- Transcriptional regulation and alternative splicing cooperate in muscle fiber-type specification in flies and mammals.Experimental cell research · 2014Review
- Tracking unfolding and refolding reactions of single proteins using atomic force microscopy methods.Methods (San Diego, Calif.) · 2013Article
- Molecular analysis of the muscle protein projectin in Lepidoptera.Journal of insect science (Online) · 2013Article
- Genetic elevation of sphingosine 1-phosphate suppresses dystrophic muscle phenotypes in Drosophila.Development (Cambridge, England) · 2013Article
- Electron microscopy and 3D reconstruction reveals filamin Ig domain binding to F-actin.Journal of molecular biology · 2012Article
- Force-clamp analysis techniques give highest rank to stretched exponential unfolding kinetics in ubiquitin.Biophysical journal · 2012Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Projectin and kettin are titin-like proteins mainly responsible for the high passive stiffness of insect indirect flight muscles, which is needed to generate oscillatory work during flight. Here we report the mechanical properties of kettin and projectin by single-molecule force spectroscopy. Force-extension and force-clamp curves obtained from Lethocerus projectin and Drosophila recombinant projectin or kettin fragments revealed that fibronectin type III domains in projectin are mechanically weaker (unfolding force, F(u) approximately 50-150 pN) than Ig-domains (F(u) approximately 150-250 pN). Among Ig domains in Sls/kettin, the domains near the N terminus are less stable than those near the C terminus. Projectin domains refolded very fast [85% at 15 s(-1) (25 degrees C)] and even under high forces (15-30 pN). Temperature affected the unfolding forces with a Q(10) of 1.3, whereas the refolding speed had a Q(10) of 2-3, probably reflecting the cooperative nature of the folding mechanism. High bending rigidities of projectin and kettin indicated that straightening the proteins requires low forces. Our results suggest that titin-like proteins in indirect flight muscles could function according to a folding-based-spring mechanism.
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