ArticleNature structural & molecular biology2017
Mechanochemical evolution of the giant muscle protein titin as inferred from resurrected proteins.
Article in Nature structural & molecular biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 41 citations in OpenAlex.
- Ancient enzymes, new biotechnology applications.Nature reviews. Molecular cell biology · 2026Article
- Article
- A resurrected ancestor of Cas12a expands target access and substrate recognition for nucleic acid editing and detection.Nature biotechnology · 2025Article
- Evolution of CRISPR-associated endonucleases as inferred from resurrected proteins.Nature microbiology · 2023Article
- Protein nanomechanics in biological context.Biophysical reviews · 2021Review
- Ancestral Sequence Reconstruction: From Chemical Paleogenetics to Maximum Likelihood Algorithms and Beyond.Journal of molecular evolution · 2021Article
- The Mechanical Power of Titin Folding.Cell reports · 2019Article
- Evolution of the Highly Repetitive PEVK Region of Titin Across Mammals.G3 (Bethesda, Md.) · 2019Article
- Redox regulation of protein nanomechanics in health and disease: Lessons from titin.Redox biology · 2019Review
- Structural diversity in the atomic resolution 3D fingerprint of the titin M-band segment.PloS one · 2019Article
- Highly thermostable carboxylic acid reductases generated by ancestral sequence reconstruction.Communications biology · 2019Article
- Disulfide isomerization reactions in titin immunoglobulin domains enable a mode of protein elasticity.Nature communications · 2018Article
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Authors and funding
10 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sarcomere-based structure of muscles is conserved among vertebrates; however, vertebrate muscle physiology is extremely diverse. A molecular explanation for this diversity and its evolution has not been proposed. We use phylogenetic analyses and single-molecule force spectroscopy (smFS) to investigate the mechanochemical evolution of titin, a giant protein responsible for the elasticity of muscle filaments. We resurrect eight-domain fragments of titin corresponding to the common ancestors to mammals, sauropsids, and tetrapods, which lived 105-356 Myr ago, and compare them with titin fragments from some of their modern descendants. We demonstrate that the resurrected titin molecules are rich in disulfide bonds and display high mechanical stability. These mechanochemical elements have changed over time, creating a paleomechanical trend that seems to correlate with animal body size, allowing us to estimate the sizes of extinct species. We hypothesize that mechanical adjustments in titin contributed to physiological changes that allowed the muscular development and diversity of modern tetrapods.
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