ArticleNucleic acids research2012
Importance of the NCp7-like domain in the recognition of pre-let-7g by the pluripotency factor Lin28.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 34 citations in OpenAlex.
- Lin-28 homologue A (LIN28A) promotes cell cycle progression via regulation of cyclin-dependent kinase 2 (CDK2), cyclin D1 (CCND1), and cell division cycle 25 homolog A (CDC25A) expression in cancer.The Journal of biological chemistry · 2012Trial
- Structural basis for activity switching in polymerases determining the fate of let-7 pre-miRNAs.Nature structural & molecular biology · 2024Article
- Regulating Protein-RNA Interactions: Advances in Targeting the LIN28/Let-7 Pathway.International journal of molecular sciences · 2024Review
- Substrate promiscuity of Dicer toward precursors of the let-7 family and their 3'-end modifications.Cellular and molecular life sciences : CMLS · 2024Article
- Review
- Differential Regulation ofMolecular cancer research : MCR · 2018Article
- Oncogenic mechanisms of Lin28 in breast cancer: new functions and therapeutic opportunities.Oncotarget · 2017Review
- 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
- An RNA-binding Protein, Lin28, Recognizes and Remodels G-quartets in the MicroRNAs (miRNAs) and mRNAs It Regulates.The Journal of biological chemistry · 2015Article
- A novel mechanism of LIN-28 regulation of let-7 microRNA expression revealed by in vivo HITS-CLIP in C. elegans.RNA (New York, N.Y.) · 2015Article
- Functional roles of N-terminal and C-terminal domains in the overall activity of a novel single-stranded DNA binding protein of Deinococcus radiodurans.FEBS open bio · 2015Article
- Short loop-targeting oligoribonucleotides antagonize Lin28 and enable pre-let-7 processing and suppression of cell growth in let-7-deficient cancer cells.Nucleic acids research · 2015Article
- LIN28A marks the spermatogonial progenitor population and regulates its cyclic expansion.Stem cells (Dayton, Ohio) · 2014Article
- Stepwise assembly of multiple Lin28 proteins on the terminal loop of let-7 miRNA precursors.Nucleic acids research · 2014Article
- Mechanisms of Lin28-mediated miRNA and mRNA regulation--a structural and functional perspective.International journal of molecular sciences · 2013Review
- Identification of LIN28B-bound mRNAs reveals features of target recognition and regulation.RNA biology · 2013Article
- LIN28 binds messenger RNAs at GGAGA motifs and regulates splicing factor abundance.Molecular cell · 2012Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The pluripotency factor Lin28 is a highly conserved protein comprising a unique combination of RNA-binding motifs, an N-terminal cold-shock domain and a C-terminal region containing two retroviral-type CCHC zinc-binding domains. An important function of Lin28 is to inhibit the biogenesis of the let-7 family of microRNAs through a direct interaction with let-7 precursors. Here, we systematically characterize the determinants of the interaction between Lin28 and pre-let-7 g by investigating the effect of protein and RNA mutations on in vitro binding. We determine that Lin28 binds with high affinity to the extended loop of pre-let-7 g and that its C-terminal domain contributes predominantly to the affinity of this interaction. We uncover remarkable similarities between this C-terminal domain and the NCp7 protein of HIV-1, not only in terms of primary structure but also in their modes of RNA binding. This NCp7-like domain of Lin28 recognizes a G-rich bulge within pre-let-7 g, which is adjacent to one of the Dicer cleavage sites. We hypothesize that the NCp7-like domain initiates RNA binding and partially unfolds the RNA. This partial unfolding would then enable multiple copies of Lin28 to bind the extended loop of pre-let-7 g and protect the RNA from cleavage by the pre-microRNA processing enzyme Dicer.
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