Self-organized networks: Darwinian evolution of dynein rings, stalks, and stalk heads
| Autor: | James C. Phillips |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2020 |
| Předmět: |
0301 basic medicine
Protein Conformation Dynein Kinesins macromolecular substances Myosins Microtubules 01 natural sciences Biophysical Phenomena Evolution Molecular Motor protein 03 medical and health sciences Adenosine Triphosphate Tubulin 0103 physical sciences Molecular motor Animals Amino Acid Sequence Letters 010306 general physics Cytoskeleton Actin Coiled coil Multidisciplinary biology Chemistry Dyneins Biological Sciences Actins 030104 developmental biology biology.protein Biophysics Kinesin Genetic Fitness |
| Zdroj: | Proc Natl Acad Sci U S A |
| Popis: | Cytoskeletons are self-organized networks based on polymerized proteins: actin, tubulin, and driven by motor proteins, such as myosin, kinesin, and dynein. Their positive Darwinian evolution enables them to approach optimized functionality (self-organized criticality). Dynein has three distinct titled subunits, but how these units connect to function as a molecular motor is mysterious. Dynein binds to tubulin through two coiled coil stalks and a stalk head. The energy used to alter the head binding and propel cargo along tubulin is supplied by ATP at a ring 1,500 amino acids away. Here, we show how many details of this extremely distant interaction are explained by water waves quantified by thermodynamic scaling. Water waves have shaped all proteins throughout positive Darwinian evolution, and many aspects of long-range water–protein interactions are universal (described by self-organized criticality). Dynein water waves resembling tsunami produce nearly optimal energy transport over 1,500 amino acids along dynein’s one-dimensional peptide backbone. More specifically, this paper identifies many similarities in the function and evolution of dynein compared to other cytoskeleton proteins such as actin, myosin, and tubulin. |
| Databáze: | OpenAIRE |
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