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The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei
Open accessAbstract
SUMMARY Many DNA and RNA regulatory proteins contain polypeptide domains that are unstructured when analyzed in cell lysates. These domains are typified by an over-representation of a limited number of amino acids and have been termed prion-like, intrinsically disordered or low complexity (LC) domains. When incubated at high concentration, certain of these LC domains polymerize into labile, amyloid-like fibers. Here we report methods allowing the generation of a molecular footprint of the polymeric state of the LC domain of hnRNPA2. By deploying this footprinting technique to probe the structure of the native hnRNPA2 protein present in isolated nuclei, we offer evidence that its LC domain exists in a similar conformation as that described for recombinant polymers of the protein. These observations favor biologic utility to the polymerization of LC domains in the pathway of information transfer from gene to message to protein.
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Metadata
- Authors
- Xiang, S., Kato, M., Wu, L. C., Lin, Y., Ding, M., Zhang, Y., Yu, Y., & McKnight, S. L.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2015-11
- Volume
- 163
- Issue
- 4
- Pages
- 829-839
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2100383597
- Cited by
- 298
- References
- 5
- FWCI
- 12.74
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Xiang, S., Kato, M., Wu, L. C., Lin, Y., Ding, M., Zhang, Y., Yu, Y., & McKnight, S. L. (2015). The LC Domain of hnRNPA2 Adopts Similar Conformations in Hydrogel Polymers, Liquid-like Droplets, and Nuclei. Cell. https://doi.org/10.1016/j.cell.2015.10.040
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