Please use this identifier to cite or link to this item:http://hdl.handle.net/20.500.12105/9931
Mechanochemical evolution of the giant muscle protein titin as inferred from resurrected proteins
Nat Struct Mol Biol. 2017; 24(8):652-657
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.
Animals | Connectin | Disulfides | Phylogeny | Spectrum Analysis | Vertebrates | Chemical Phenomena | Evolution, Molecular | Mechanical Phenomena
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