ArticleRNA (New York, N.Y.)2018
Highly efficient in vitro translation of authentic affinity-purified messenger ribonucleoprotein complexes.
Article in RNA (New York, N.Y.), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- Optimizing Human Cell-Free System for Efficient Protein Production.Journal of microbiology and biotechnology · 2025Article
- UPF1 ATPase autoinhibition and activation modulate RNA binding kinetics and NMD efficiency.Nucleic acids research · 2024Article
- Purification of In Vivo or In Vitro-Assembled RNA-Protein Complexes by RNA Centric Methods.Advances in experimental medicine and biology · 2024Article
- UPF1 ATPase autoinhibition and activation modulate RNA binding kinetics and NMD efficiency.bioRxiv : the preprint server for biology · 2023Article
- Human-rabbit Hybrid Translation System to Explore the Function of Modified Ribosomes.Bio-protocol · 2023Article
- General Strategies for RNA X-ray Crystallography.Molecules (Basel, Switzerland) · 2023Review
- An Innovative PTD-IVT-mRNA Delivery Platform for CAR Immunotherapy of ErbB(+) Solid Tumor Neoplastic Cells.Biomedicines · 2022Article
- An alternative UPF1 isoform drives conditional remodeling of nonsense-mediated mRNA decay.The EMBO journal · 2022Article
- Article
- In vivo, in vitro and in silico: an open space for the development of microbe-based applications of synthetic biology.Microbial biotechnology · 2022Article
- Human NMD ensues independently of stable ribosome stalling.Nature communications · 2020Article
- The RNA-binding protein PTBP1 promotes ATPase-dependent dissociation of the RNA helicase UPF1 to protect transcripts from nonsense-mediated mRNA decay.The Journal of biological chemistry · 2020Article
- Why Nature Chose Potassium.Journal of molecular evolution · 2019Review
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
Cell-free systems are widely used to study mechanisms and regulation of translation, but the use of in vitro transcribed (IVT) mRNAs as translation substrates limits their efficiency and utility. Here, we present an approach for in vitro translation of messenger ribonucleoprotein (mRNP) complexes affinity purified in association with tagged mRNAs expressed in mammalian cells. We show that in vitro translation of purified mRNPs is much more efficient than that achieved using standard IVT mRNA substrates and is compatible with physiological ionic conditions. The high efficiency of affinity-purified mRNP in vitro translation is attributable to both copurified protein components and proper mRNA processing and modification. Further, we use translation inhibitors to show that translation of purified mRNPs consists of separable phases of run-off elongation by copurified ribosomes and de novo initiation by ribosomes present in the translation extracts. We expect that this in vitro system will enhance mechanistic studies of eukaryotic translation and translation-associated processes by allowing the use of endogenous mRNPs as translation substrates under physiological buffer conditions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.