Ribosomes are large complexes of RNA and protein that perform the essential task of protein synthesis in the cell. Ribosomes also serve as the initiation point for several translation-associated functions. To perform these tasks efficiently, ribosomes interact with a myriad of nonribosomal proteins and RNAs. Given that most of these interactions are transient, purification of the interacting factors in complex with the ribosome can be a challenging undertaking. Here, we review methods commonly used to isolate ribosomes and study ribosome-associated factors. We also discuss crucial parameters for designing and executing ribosome association studies. Finally, we present a detailed protocol for reporter based enrichment assays that are employed to selectively isolate ribosomes translating a particular message of interest. These protocols can be used to study a wide range of ribosome-associated functions. © 2012 Springer Science+Business Media, LLC.
CITATION STYLE
Mehta, P., Woo, P., Venkataraman, K., & Karzai, A. W. (2012). Ribosome purification approaches for studying interactions of regulatory proteins and rnas with the ribosome. Methods in Molecular Biology. https://doi.org/10.1007/978-1-61779-949-5_18
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