Abstract
In humans, the RNA exosome consists of an enzymatically inactive nine-subunit core, with ribonucleolytic activity contributed by additional components. Several cofactor complexes also interact with the exosome—these enable the recruitment of, and specify the activity upon, diverse substrates. Affinity capture coupled with mass spectrometry has proven to be an effective means to identify the compositions of RNA exosomes and their cofactor complexes: here, we describe a general experimental strategy for proteomic characterization of macromolecular complexes, applied to the exosome and an affiliated adapter protein, ZC3H18.
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01 December 2020
A correction has been published.
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Acknowledgments
This work is supported in part by National Institutes of Health grant R01GM126170. We gratefully acknowledge Ms. Hua Jiang and Ms. Kelly Molloy for additional proofreading.
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Winczura, K., Domanski, M., LaCava, J. (2020). Affinity Proteomic Analysis of the Human Exosome and Its Cofactor Complexes. In: LaCava, J., Vaňáčová, Š. (eds) The Eukaryotic RNA Exosome. Methods in Molecular Biology, vol 2062. Humana, New York, NY. https://doi.org/10.1007/978-1-4939-9822-7_15
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DOI: https://doi.org/10.1007/978-1-4939-9822-7_15
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