ArticleProceedings of the National Academy of Sciences of the United States of America2011
An intrinsically disordered C terminus allows the La protein to assist the biogenesis of diverse noncoding RNA precursors.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 42 citations in OpenAlex.
- Article
- Use of tRNA-Mediated Suppression to Assess RNA Chaperone Function.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Analysis of tRNA Aminoacylation by Northern Blotting and Multiplex Small RNA-Seq.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Key RNA-binding domains in the La protein establish tRNA modification levels in Trypanosoma brucei.Nucleic acids research · 2025Article
- A tRNA gene potential to activate interferon signaling involves selective termination and is suppressible by La protein/SSB.Nucleic acids research · 2025Article
- The fission yeast methyl phosphate capping enzyme Bmc1 guides 2'-O-methylation of the U6 snRNA.Nucleic acids research · 2023Article
- The La-related proteins: structures and interactions of a versatile superfamily of RNA-binding proteins.RNA biology · 2021Review
- La proteins couple use of sequence-specific and non-specific binding modes to engage RNA substrates.RNA biology · 2021Review
- Role of the RNA-binding protein La in cancer pathobiology.RNA biology · 2021Review
- Review
- Proteins That Chaperone RNA Regulation.Microbiology spectrum · 2018Review
- Noncoding RNA Surveillance: The Ends Justify the Means.Chemical reviews · 2018Review
- The RNA chaperone La promotes pre-tRNA maturation via indiscriminate binding of both native and misfolded targets.Nucleic acids research · 2017Article
- The La and related RNA-binding proteins (LARPs): structures, functions, and evolving perspectives.Wiley interdisciplinary reviews. RNA · 2017Review
- La Deletion from Mouse Brain Alters Pre-tRNA Metabolism and Accumulation of Pre-5.8S rRNA, with Neuron Death and Reactive Astrocytosis.Molecular and cellular biology · 2017Article
- Factors That Shape Eukaryotic tRNAomes: Processing, Modification and Anticodon-Codon Use.Biomolecules · 2017Review
- The Rrp6 C-terminal domain binds RNA and activates the nuclear RNA exosome.Nucleic acids research · 2017Article
- An RNA Binding Peptide Consisting of Four Types of Amino Acid by in Vitro Selection Using cDNA Display.ACS omega · 2016Article
- SUMO-Modification of the La Protein Facilitates Binding to mRNA In Vitro and in Cells.PloS one · 2016Article
- Novel RNA chaperone domain of RNA-binding protein La is regulated by AKT phosphorylation.Nucleic acids research · 2015Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The La protein binds the 3' ends of many newly synthesized noncoding RNAs, protecting these RNAs from nucleases and influencing folding, maturation, and ribonucleoprotein assembly. Although 3' end binding by La involves the N-terminal La domain and adjacent RNA recognition motif (RRM), the mechanisms by which La stabilizes diverse RNAs from nucleases and assists subsequent events in their biogenesis are unknown. Here we report that a conserved feature of La proteins, an intrinsically disordered C terminus, is required for the accumulation of certain noncoding RNA precursors and for the role of the Saccharomyces cerevisiae La protein Lhp1p in assisting formation of correctly folded pre-tRNA anticodon stems in vivo. Footprinting experiments using purified Lhp1p reveal that the C terminus is required to protect a pre-tRNA anticodon stem from chemical modification. Although the C terminus of Lhp1p is hypersensitive to proteases in vitro, it becomes protease-resistant upon binding pre-tRNAs, U6 RNA, or pre-5S rRNA. Thus, while high affinity binding to 3' ends requires the La domain and RRM, a conformationally flexible C terminus allows La to interact productively with a diversity of noncoding RNA precursors. We propose that intrinsically disordered domains adjacent to well characterized RNA-binding motifs in other promiscuous RNA-binding proteins may similarly contribute to the ability of these proteins to influence the cellular fates of multiple distinct RNA targets.
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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.