ArticleStructure (London, England : 1993)2011
Alternate modes of cognate RNA recognition by human PUMILIO proteins.
Article in Structure (London, England : 1993), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 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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52 citing papers in PubMed, 93 citations in OpenAlex.
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- Effective in vivo RNA base editing via engineered cytidine deaminase APOBECs fused with PUF proteins.Nature communications · 2025Article
- Accurate in silico predictions of modified RNA interactions to a prototypical RNA-binding protein with λ-dynamics.RNA (New York, N.Y.) · 2025Article
- PUM2 binds SARS-CoV-2 RNA and PUM1 mildly reduces viral RNA levels, but neither protein affects progeny virus production.The Journal of general virology · 2025Article
- Synthetic biomolecular condensates enhance translation from a target mRNA in living cells.Nature chemistry · 2025Article
- RNAelem: an algorithm for discovering sequence-structure motifs in RNA bound by RNA-binding proteins.Bioinformatics advances · 2024Article
- RNA molecular recording with an engineered RNA deaminase.Nature methods · 2023Article
- PIE-seq: identifying RNA-binding protein targets by dual RNA-deaminase editing and sequencing.Nature communications · 2023Article
- Mammalian pumilio proteins control cellular morphology, migration, and adhesion.Scientific reports · 2023Article
- Two distinct binding modes provide the RNA-binding protein RbFox with extraordinary sequence specificity.Nature communications · 2023Article
- A comprehensive thermodynamic model for RNA binding by the Saccharomyces cerevisiae Pumilio protein PUF4.Nature communications · 2022Article
- Bipartite interaction sites differentially modulate RNA-binding affinity of a protein complex essential for germline stem cell self-renewal.Nucleic acids research · 2022Article
- Structural recognition of the mRNA 3' UTR by PUF-8 restricts the lifespan of C. elegans.Nucleic acids research · 2021Article
- Expanding the binding specificity for RNA recognition by a PUF domain.Nature communications · 2021Article
- Human Pumilio proteins directly bind the CCR4-NOT deadenylase complex to regulate the transcriptome.RNA (New York, N.Y.) · 2021Article
- Principles of mRNA control by human PUM proteins elucidated from multimodal experiments and integrative data analysis.RNA (New York, N.Y.) · 2020Article
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2 authors at 1 institution in 1 country.
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Abstract
Human PUMILIO1 (PUM1) and PUMILIO2 (PUM2) are members of the PUMILIO/FBF (PUF) family that regulate specific target mRNAs posttranscriptionally. Recent studies have identified mRNA targets associated with human PUM1 and PUM2. Here, we explore the structural basis of natural target RNA recognition by human PUF proteins through crystal structures of the RNA-binding domains of PUM1 and PUM2 in complex with four cognate RNA sequences, including sequences from p38α and erk2 MAP kinase mRNAs. We observe three distinct modes of RNA binding around the fifth RNA base, two of which are different from the prototypical 1 repeat:1 RNA base binding mode previously identified with model RNA sequences. RNA-binding affinities of PUM1 and PUM2 are not affected dramatically by the different binding modes in vitro. However, these modes of binding create structurally variable recognition surfaces that suggest a mechanism in vivo for recruitment of downstream effector proteins defined by the PUF:RNA complex.
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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.