Journal article
Affinity Proteomic Analysis of the Human Exosome and Its Cofactor Complexes.
- Winczura K School of Biosciences, College of Life and Environmental Sciences, University of Birmingham, Birmingham, UK.
- Domanski M Department of Chemistry and Biochemistry, University of Bern, Bern, Switzerland.
- LaCava J Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, NY, USA. jlacava@rockefeller.edu.
- 2019-11-27
Published in:
- Methods in molecular biology (Clifton, N.J.). - 2020
English
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.
- Language
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- English
- Open access status
- closed
- Identifiers
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- DOI 10.1007/978-1-4939-9822-7_15
- PMID 31768983
- Persistent URL
- https://sonar.ch/global/documents/47306
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