ArticleProceedings of the National Academy of Sciences of the United States of America2016
PGL germ granule assembly protein is a base-specific, single-stranded RNase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
What it found
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Who cites it
17 citing papers in PubMed, 26 citations in OpenAlex.
- Germ granule components regulate endosomal switching during the oocyte-to-embryo transition in Caenorhabditis elegans.Communications biology · 2026Article
- The dynamic evolution of panarthropod germ cell specification mechanisms.Development (Cambridge, England) · 2026Review
- Phase separation of PGL-3 driven by structured domains that oligomerize and interact with RGG motifs.EMBO reports · 2026Article
- eIF4E assembly intobioRxiv : the preprint server for biology · 2025Article
- How germ granules promote germ cell fate.Nature reviews. Genetics · 2024Review
- Looking at Biomolecular Interactions through the Lens of Correlated Fluorescence Microscopy and Optical Tweezers.International journal of molecular sciences · 2023Review
- Structural and functional organization of germ plasm condensates.The Biochemical journal · 2022Review
- Review
- Nuage condensates: accelerators or circuit breakers for sRNA silencing pathways?RNA (New York, N.Y.) · 2022Review
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- Article
- C. elegans germ granules require both assembly and localized regulators for mRNA repression.Nature communications · 2021Article
- TOR Signaling inGenetics · 2019Review
- Membraneless organelles: P granules in Caenorhabditis elegans.Traffic (Copenhagen, Denmark) · 2019Review
- The P Granules of C. elegans: A Genetic Model for the Study of RNA-Protein Condensates.Journal of molecular biology · 2018Review
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- An effective Caenorhabditis elegans CRISPR training module for high school and undergraduate summer research experiences in molecular biology.Biochemistry and molecular biology education : a bimonthly publication of the International Union of Biochemistry and Molecular BiologyArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Cellular RNA-protein (RNP) granules are ubiquitous and have fundamental roles in biology and RNA metabolism, but the molecular basis of their structure, assembly, and function is poorly understood. Using nematode "P-granules" as a paradigm, we focus on the PGL granule scaffold protein to gain molecular insights into RNP granule structure and assembly. We first identify a PGL dimerization domain (DD) and determine its crystal structure. PGL-1 DD has a novel 13 α-helix fold that creates a positively charged channel as a homodimer. We investigate its capacity to bind RNA and discover unexpectedly that PGL-1 DD is a guanosine-specific, single-stranded endonuclease. Discovery of the PGL homodimer, together with previous results, suggests a model in which the PGL DD dimer forms a fundamental building block for P-granule assembly. Discovery of the PGL RNase activity expands the role of RNP granule assembly proteins to include enzymatic activity in addition to their job as structural scaffolds.
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Registered trials
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.