ArticleNucleic acids research1997
Identification of proteins binding specifically to the 3'-untranslated region of granulocyte/macrophage-colony stimulating factor mRNA.
Article in Nucleic acids research, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
4 citing papers in PubMed.
- Arabidopsis mTERF9 protein promotes chloroplast ribosomal assembly and translation by establishing ribonucleoprotein interactions in vivo.Nucleic acids research · 2021Article
- Identification of tobacco proteins associated with the stem-loop 1 RNAs of Potato virus X.Molecules and cells · 2012Article
- The Drosophila Bruno paralogue Bru-3 specifically binds the EDEN translational repression element.Nucleic acids research · 2004Article
- The enhancer of decapping proteins, Edc1p and Edc2p, bind RNA and stimulate the activity of the decapping enzyme.RNA (New York, N.Y.) · 2003Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The 3'-untranslated region of granulocyte/macrophage colony-stimulating factor (GM-CSF) mRNA contributes to the post-transcriptional regulation of gene expression. Degradation is partly mediated by adenosine- uridine-rich sequence elements (ARE), which serve as binding sites for specific proteins. Stabilization of RNA by phytohemagglutinin and concanavalin A treatment is dependent on regulatory sequence elements upstream of ARE. We have performed northwestern blot and filter binding assays using cell extracts and RNA sequences containing or lacking ARE. Murine and human T cell extracts (EL-4 and Jurkat) yielded two specific proteins of 93 and 94 kDa, respectively, that were binding to sequences upstream of ARE. Within this region, the human and murine RNA do not share any obvious sequence identity, yet both are target sites for the binding proteins. The smallest RNA fragments protected by the proteins from RNase A digestion, were 44 in the murine, and 38 ribonucleotides long in the human sequence. The binding activity of the 94 kDa protein derived from human Jurkat cells could be enhanced by phytohemagglutinin. The interaction with regulatory mRNA sequences and the responsiveness to phytohemagglutinin suggests that the proteins are involved in controlling GM-CSF mRNA turnover.
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