ArticleRNA (New York, N.Y.)2006
Affinity purification of eukaryotic 48S initiation complexes.
Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Purification of In Vivo or In Vitro-Assembled RNA-Protein Complexes by RNA Centric Methods.Advances in experimental medicine and biology · 2024Article
- eIF3d is an mRNA cap-binding protein that is required for specialized translation initiation.Nature · 2016Article
- Functional analysis of Kaposi's sarcoma-associated herpesvirus vFLIP expression reveals a new mode of IRES-mediated translation.RNA (New York, N.Y.) · 2014Article
- Norovirus translation requires an interaction between the C Terminus of the genome-linked viral protein VPg and eukaryotic translation initiation factor 4G.The Journal of biological chemistry · 2014Article
- IRES-mediated translation of cellular messenger RNA operates in eIF2α- independent manner during stress.Nucleic acids research · 2012Article
- A conserved structure within the HIV gag open reading frame that controls translation initiation directly recruits the 40S subunit and eIF3.Nucleic acids research · 2011Article
- In vivo expression and purification of aptamer-tagged small RNA regulators.Nucleic acids research · 2009Article
- Giardiavirus internal ribosome entry site has an apparently unique mechanism of initiating translation.PloS one · 2009Article
- Conserved functional domains and a novel tertiary interaction near the pseudoknot drive translational activity of hepatitis C virus and hepatitis C virus-like internal ribosome entry sites.Nucleic acids research · 2009Article
- HCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assembly.The EMBO journal · 2007Article
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3 authors.
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Abstract
In vitro assembly of translation initiation complexes from higher eukaryotes requires purification of ribosomal subunits, eukaryotic initiation factors, and initiator tRNA from natural sources, and therefore yields only limited material for functional and structural studies. Here we describe a robust, affinity chromatography-based purification of eukaryotic 48S initiation complexes from rabbit reticulocyte lysate (RRL), which significantly reduces the number of individual purification steps. Hybrid RNA molecules, consisting of either a canonical 5' UTR or an internal ribosome entry site (IRES) RNA followed by a short open reading frame and a streptomycin aptamer sequence, are incubated in RRL to form 48S complexes. The assembly reaction is then applied to a dihydrostreptomycin-sepharose column; bound complexes are washed and specifically eluted upon addition of streptomycin. The eluted fractions are further purified by centrifugation through a sucrose density gradient to yield pure 48S particles. Using this purification scheme, properly assembled IRES-mediated as well as canonical 48S complexes were purified in milligram quantities.
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