ArticleProceedings of the National Academy of Sciences of the United States of America2015
Structural basis for the activation of the C. elegans noncanonical cytoplasmic poly(A)-polymerase GLD-2 by GLD-3.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 26 citations in OpenAlex.
- A higher order PUF complex is central to regulation of C. elegans germline stem cells.Nature communications · 2025Article
- A higher order PUF complex is central to regulation ofbioRxiv : the preprint server for biology · 2024Article
- Germline immortality relies on TRIM32-mediated turnover of a maternal mRNA activator inScience advances · 2022Article
- Gld2 activity and RNA specificity is dynamically regulated by phosphorylation and interaction with QKI-7.RNA biology · 2021Article
- Review
- Functions and mechanisms of RNA tailing by metazoan terminal nucleotidyltransferases.Wiley interdisciplinary reviews. RNA · 2021Review
- Structures of mammalian GLD-2 proteins reveal molecular basis of their functional diversity in mRNA and microRNA processing.Nucleic acids research · 2020Article
- A tale of non-canonical tails: gene regulation by post-transcriptional RNA tailing.Nature reviews. Molecular cell biology · 2020Review
- Structural and Functional Analyses of the FAM46C/Plk4 Complex.Structure (London, England : 1993) · 2020Article
- FAM46B is a prokaryotic-like cytoplasmic poly(A) polymerase essential in human embryonic stem cells.Nucleic acids research · 2020Article
- The RNA-binding protein QKI-7 recruits the poly(A) polymerase GLD-2 for 3' adenylation and selective stabilization of microRNA-122.The Journal of biological chemistry · 2020Article
- Stage-specific combinations of opposing poly(A) modifying enzymes guide gene expression during early oogenesis.Nucleic acids research · 2019Article
- Structural Basis for Target-Directed MicroRNA Degradation.Molecular cell · 2019Article
- Gld2 activity is regulated by phosphorylation in the N-terminal domain.RNA biology · 2019Article
- A single KH domain in Bicaudal-C links mRNA binding and translational repression functions to maternal development.Development (Cambridge, England) · 2019Article
- Terminal nucleotidyl transferases (TENTs) in mammalian RNA metabolism.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018Review
- Article
- Multi-domain utilization by TUT4 and TUT7 in control of let-7 biogenesis.Nature structural & molecular biology · 2017Article
- Polyadenylation is the key aspect of GLD-2 function inRNA (New York, N.Y.) · 2017Article
- Structural basis for the antagonistic roles of RNP-8 and GLD-3 in GLD-2 poly(A)-polymerase activity.RNA (New York, N.Y.) · 2016Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Caenorhabditis elegans germ-line development defective (GLD)-2-GLD-3 complex up-regulates the expression of genes required for meiotic progression. GLD-2-GLD-3 acts by extending the short poly(A) tail of germ-line-specific mRNAs, switching them from a dormant state into a translationally active state. GLD-2 is a cytoplasmic noncanonical poly(A) polymerase that lacks the RNA-binding domain typical of the canonical nuclear poly(A)-polymerase Pap1. The activity of C. elegans GLD-2 in vivo and in vitro depends on its association with the multi-K homology (KH) domain-containing protein, GLD-3, a homolog of Bicaudal-C. We have identified a minimal polyadenylation complex that includes the conserved nucleotidyl-transferase core of GLD-2 and the N-terminal domain of GLD-3, and determined its structure at 2.3-Å resolution. The structure shows that the N-terminal domain of GLD-3 does not fold into the predicted KH domain but wraps around the catalytic domain of GLD-2. The picture that emerges from the structural and biochemical data are that GLD-3 activates GLD-2 both indirectly by stabilizing the enzyme and directly by contributing positively charged residues near the RNA-binding cleft. The RNA-binding cleft of GLD-2 has distinct structural features compared with the poly(A)-polymerases Pap1 and Trf4. Consistently, GLD-2 has distinct biochemical properties: It displays unusual specificity in vitro for single-stranded RNAs with at least one adenosine at the 3' end. GLD-2 thus appears to have evolved specialized nucleotidyl-transferase properties that match the 3' end features of dormant cytoplasmic mRNAs.
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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.