ArticleNucleic acids research2014
Stepwise assembly of multiple Lin28 proteins on the terminal loop of let-7 miRNA precursors.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 16 citations in OpenAlex.
- Review
- Lin28a uses distinct mechanisms of binding to RNA and affects miRNA levels positively and negatively.RNA (New York, N.Y.) · 2017Article
- Identification of small molecule inhibitors of the Lin28-mediated blockage of pre-let-7g processing.Organic & biomolecular chemistry · 2016Article
- ARiBo pull-down for riboproteomic studies based on label-free quantitative mass spectrometry.RNA (New York, N.Y.) · 2016Article
- Human Lin28 Forms a High-Affinity 1:1 Complex with the 106~363 Cluster miRNA miR-363.Biochemistry · 2016Article
- miR-26a suppresses EMT by disrupting the Lin28B/let-7d axis: potential cross-talks among miRNAs in IPF.Journal of molecular medicine (Berlin, Germany) · 2016Article
- High DNA melting activity of extremophyteBiochemistry and biophysics reports · 2016Article
- Biogenesis and regulation of the let-7 miRNAs and their functional implications.Protein & cell · 2016Review
- The many faces of Dicer: the complexity of the mechanisms regulating Dicer gene expression and enzyme activities.Nucleic acids research · 2015Review
- The cell survival pathways of the primordial RNA-DNA complex remain conserved in the extant genomes and may function as proto-oncogenes.European journal of microbiology & immunology · 2015Review
- SET7/9 methylation of the pluripotency factor LIN28A is a nucleolar localization mechanism that blocks let-7 biogenesis in human ESCs.Cell stem cell · 2014Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Lin28 inhibits the biogenesis of let-7 miRNAs through direct interactions with let-7 precursors. Previous studies have described seemingly inconsistent Lin28 binding sites on pre-let-7 RNAs. Here, we reconcile these data by examining the binding mechanism of Lin28 to the terminal loop of pre-let-7g (TL-let-7g) using biochemical and biophysical methods. First, we investigate Lin28 binding to TL-let-7g variants and short RNA fragments and identify three independent binding sites for Lin28 on TL-let-7g. We then determine that Lin28 assembles in a stepwise manner on TL-let-7g to form a stable 1:3 complex. We show that the cold-shock domain (CSD) of Lin28 is responsible for remodelling the terminal loop of TL-let-7g, whereas the NCp7-like domain facilitates the initial binding of Lin28 to TL-let-7g. This stable binding of multiple Lin28 molecules to the terminal loop of pre-let-7g extends to other precursors of the let-7 family, but not to other pre-miRNAs tested. We propose a model for stepwise assembly of the 1:1, 1:2 and 1:3 pre-let-7g/Lin28 complexes. Stepwise multimerization of Lin28 on pre-let-7 is required for maximum inhibition of Dicer cleavage for a least one member of the let-7 family and may be important for orchestrating the activity of the several factors that regulate let-7 biogenesis.
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Registered trials
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