Journal
NATURE
Volume 555, Issue 7694, Pages 61-+Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nature25762
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Funding
- Swiss National Science Foundation
- Danish Council for Independent Research [4181-00344]
- Novo Nordisk Foundation
- Carlsberg Foundation
- Intramural Research Program of the National Institute of Diabetes and Digestive and Kidney Diseases of the National Institutes of Health
- Novo Nordisk Fonden [NNF15OC0013972, NNF15OC0016670] Funding Source: researchfish
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Molecular communication in biology is mediated by protein interactions. According to the current paradigm, the specificity and affinity required for these interactions are encoded in the precise complementarity of binding interfaces. Even proteins that are disordered under physiological conditions or that contain large unstructured regions commonly interact with well-structured binding sites on other biomolecules. Here we demonstrate the existence of an unexpected interaction mechanism: the two intrinsically disordered human proteins histone H1 and its nuclear chaperone prothymosin-a associate in a complex with picomolar affinity, but fully retain their structural disorder, long-range flexibility and highly dynamic character. On the basis of closely integrated experiments and molecular simulations, we show that the interaction can be explained by the large opposite net charge of the two proteins, without requiring defined binding sites or interactions between specific individual residues. Proteome-wide sequence analysis suggests that this interaction mechanism may be abundant in eukaryotes.
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