Gene Ontology annotation based on Enzyme Commission mapping
-
Automated mapping of EC numbers to GO terms for enzymatic functions
-
PGL-1 assigned EC 4.6.1.24 (guanyl-specific ribonuclease) maps to GO:0046589
-
Provides computational annotation for enzyme activities based on biochemical classification
Annotation inferences using phylogenetic trees
-
PAINT asserts descendant inheritance from experimentally supported ancestral IBD nodes. The actual Q9TZQ3 lineage is positive for helicase, mRNA binding, splicing and export; reconciling that placement with target PGL structure is an unresolved biological question.
Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
-
Automated annotation based on UniProtKB keywords and controlled vocabulary
-
Provides broad functional categories but often lacks specificity
-
Generated many of the general terms like hydrolase activity and cell differentiation for PGL-1
An isoform of eIF4E is a component of germ granules and is required for spermatogenesis in C. elegans.
-
IFE-1 (eIF4E isoform) is a P granule component that directly interacts with PGL-1
"In vitro PGL-1 interacts directly with IFE-1, but not with the other four isoforms of eIF4E."
-
IFE-1 is essential for spermatogenesis and male fertility in C. elegans
"Analysis of animals depleted of IFE-1 by RNAi shows that IFE-1 is required for spermatogenesis, specifically for efficient progression through the meiotic divisions and for the production of functional sperm, in both hermaphrodites and males."
-
PGL-1 recruits translation initiation factors like IFE-1 into P granules for translational control
"The association of IFE-1 with P granules requires the P-granule protein PGL-1."
A map of the interactome network of the metazoan C. elegans.
-
This is a genome-scale, high-throughput yeast two-hybrid interactome
map of C. elegans (Worm Interactome WI5, ~5500 interactions) and is
the source of the high-throughput protein binding (GO:0005515)
annotation for PGL-1. The cached abstract does not enumerate the
specific PGL-1 interactors, so the individual partners cannot be
traced from this record alone.
"more than 4000 interactions were identified from high-throughput, yeast two-hybrid (HT=Y2H) screens"
The PGL family proteins associate with germ granules and function redundantly in Caenorhabditis elegans germline development.
-
PGL-1 and PGL-3 function redundantly with enhanced sterility in double mutants
"pgl-1; pgl-3 (but not pgl-2; pgl-1) double-mutant hermaphrodites and males show significantly enhanced sterility at all temperatures, compared to pgl-1 alone."
-
All three PGL proteins interact with each other in vitro and form protein complexes in vivo
"All three PGL proteins interact with each other in vitro. Furthermore, PGL-1 and PGL-3 are co-immunoprecipitated from embryo extracts, indicating that they are indeed in the same protein complex in vivo."
-
Each PGL protein localizes to P granules independently but PGL-3 provides backup function for PGL-1
"Nevertheless, each PGL protein localizes to P granules independently of the other two."
The C. elegans sex determination gene laf-1 encodes a putative DEAD-box RNA helicase.
PGL proteins self associate and bind RNPs to mediate germ granule assembly in C. elegans.
-
PGL proteins autonomously form granules through self-association and RGG box-mediated RNA binding
"PGL proteins have the ability to self-associate and recruit RNPs"
-
PGL proteins serve as scaffolds that recruit other P granule components into organized structures
"Depletion of PGL proteins from early C. elegans embryos caused dispersal of other germ granule components in the cytoplasm, suggesting that PGL proteins are essential for the architecture of germ granules."
-
Two-step model where PGL proteins first bind RNPs, then self-aggregate to form granules
"we found that two functional domains of PGL proteins contribute to germ granule assembly: an RGG box for recruiting RNA and RNA-binding proteins and a self-association domain for formation of globular granules."
The disordered P granule protein LAF-1 drives phase separation into droplets with tunable viscosity and dynamics.
Loss of PGL-1 and PGL-3, members of a family of constitutive germ-granule components, promotes germline apoptosis in C. elegans.
-
PGL-1 and PGL-3 protect germ cells from excessive apoptosis during normal development
"mutants of pgl-1 and pgl-3, encoding members of a family of constitutive protein components of germline-specific P granules, showed increased germline apoptosis under both physiological and DNA-damaged conditions."
-
Loss of both proteins leads to increased CED-4 levels and enhanced germline cell death
"Furthermore, protein levels of CED-4, the Apaf-1 homolog, and cytoplasmic translocation of SIR-2.1, a Sirtuin homolog, significantly increased in pgl mutants and increased even more following UV irradiation."
-
PGL proteins regulate apoptosis by controlling subcellular localization of pro-apoptotic factors
"We conclude that PGL proteins suppress excessive germline apoptosis by repressing both the protein levels of CED-4 and the cytoplasmic translocation of SIR-2.1."
PGL germ granule assembly protein is a base-specific, single-stranded RNase.
-
PGL-1 dimerization domain has novel 13 α-helix fold creating positively charged channel as homodimer
"PGL-1 DD has a novel 13 α-helix fold that creates a positively charged channel as a homodimer."
-
PGL-1 is a guanosine-specific single-stranded endonuclease that cleaves RNA after G residues
"We investigate its capacity to bind RNA and discover unexpectedly that PGL-1 DD is a guanosine-specific, single-stranded endonuclease."
-
Discovery reveals PGL proteins have dual roles as structural scaffolds and enzymatic processors of RNA
"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."
Somatically expressed germ-granule components, PGL-1 and PGL-3, repress programmed cell death in C. elegans.
ELLI-1, a novel germline protein, modulates RNAi activity and P-granule accumulation in Caenorhabditis elegans.
The demethylase NMAD-1 regulates DNA replication and repair in the Caenorhabditis elegans germline.
PGL-1, a predicted RNA-binding component of germ granules, is essential for fertility in C. elegans.
-
PGL-1 is first identified as P granule component present at all developmental stages
"PGL-1 is a predicted RNA-binding protein that is present on germ granules at all stages of development."
-
Loss of PGL-1 causes defective P granules and sterility, particularly at elevated temperatures
"Elimination of PGL-1 results in defective germ granules and sterility."
-
Temperature sensitivity suggests germline development is inherently stress-sensitive and requires PGL-1 protection
"Interestingly, PGL-1 function is required for fertility only at elevated temperatures, suggesting that germline development is inherently sensitive to temperature."
Falcon deep research report on C. elegans pgl-1 (Q9TZQ3)
-
Recent (2023-2024) primary literature converges on PGL-1 as an RNA-binding
scaffold protein and core constituent of perinuclear P granules, used as the
canonical marker for P-granule structure and dynamics in the C. elegans germline.
"Recent primary literature frequently frames **PGL-1 as a scaffold-like, RNA-associated P-granule component/marker** used to visualize P-granule structure and dynamics. For example, Price et al. describe PGL-1 as an **RNA-binding scaffold protein** enriched in perinuclear P granules."
-
Using only the 2023-2024 corpus retrievable by falcon, PGL-1 is best supported
as a P-granule scaffold/RNP-condensate component; the guanyl-specific RNase
(EC 4.6.1.24) activity, while established by primary biochemistry (PMID:26787882),
was not retrievable in falcon's corpus and so was flagged unverified there.
"**Evidence-based conclusion:** using only retrieved sources, PGL-1 is best supported as a **P-granule scaffold/RNP-condensate component**; the **guanyl-specific RNase** function remains **insufficiently supported** in the accessible excerpts and should be treated as **unverified in this report** pending direct access to the biochemical primary paper(s)."
-
P granules are germline-enriched, RNA-rich, non-membrane-bound biomolecular
condensates that associate perinuclearly with nuclei and display liquid-like
behavior consistent with liquid-liquid phase separation (LLPS).
"In *C. elegans*, **P granules** are germline-enriched, RNA-rich, **non-membrane-bound biomolecular condensates** that associate with nuclei (perinuclear) and are implicated in RNA surveillance and small-RNA biology. P granules display liquid-like behavior (fusion/dripping/rearrangement) and are sensitive to perturbations consistent with liquid–liquid phase separation (LLPS)."
-
PGL-1 localizes to perinuclear P granules in the adult germline, positioning
germ granules adjacent to nuclear pores and nascent transcripts; high-resolution
imaging reveals a toroidal "P granule pockets" morphology in pachytene.
"A high-resolution imaging study in *Development* (Dec 2023) describes PGL-1 as a major P-granule constituent and reports a **toroidal (“P granule pockets”) morphology** in specific pachytene regions."
-
Perinuclear localization of PGL-1 depends on germ-granule organizational factors;
loss of the LOTUS-domain protein EGGD-1 disrupts architecture and disperses PGL-1
from the nuclear periphery into abnormal cytoplasmic/rachis aggregates, perturbing
small-RNA pathway organization and germline/somatic RNAome control.
"Loss of the LOTUS-domain protein **EGGD-1** disrupts perinuclear germ-granule architecture and is associated with **PGL-1 dispersal from the nuclear periphery** and formation of abnormal cytoplasmic/rachis aggregates."
-
RNA recruitment modulates PGL condensate material properties and fate: PGL-1
forms condensates with PGL-3 and SEPA-1, becomes coated by EPG-2 (linking to
selective autophagy), and RNA partitioning shifts condensates toward accumulation
rather than autophagic degradation, with ~68% of PGL granules being IFE-1-positive.
"In embryos, PGL proteins (including PGL-1) can form condensates with **SEPA-1** and become coated by **EPG-2**, linking granules to selective autophagy; RNA partitioning shifts condensates toward **accumulation** rather than degradation, illustrating a regulatory axis between RNA content, phase behavior, and proteostasis."
PGL-1 PAINT lineage and catalytic-scope check (2026-09-20)
UniProt record for PGL-1 (Q9TZQ3)
OpenAI deep research report on pgl-1 (C. elegans)
The P granule component PGL-1 promotes the localization and silencing activity of the PUF protein FBF-2 in germline stem cells.
Perinuclear P granules are the principal sites of mRNA export in adult C. elegans germ cells.
C. elegans germ granules require both assembly and localized regulators for mRNA repression.
-
An N-terminal dimerization domain contributes to PGL-1 assembly and fertility; distinct central and N-terminal domains should not be described as a solved full-length protein.
-
PGL-1-tethered mRNA repression depends on assembly and localized regulators, including WAGO-1; granule assembly alone is insufficient.
OpenScientist focused adjudication of PGL-1 fold and inherited helicase, splicing and export capacities
-
The report identifies PGL-specific RNase/scaffold architecture and lack of conventional helicase patterns, but its removal/NOT recommendations exceed the evidence. Two strict control motifs are misdescribed; the GAR1 match is limited to the RGG tail; the actual positive topology was not independently reconstructed.
-
The report explicitly concedes that noncatalytic process participation is untested and recommends a direct unwinding assay. These caveats are retained rather than converting motif or localization observations into experimental negatives.
Reproducible PGL-1 motif and InterPro-domain audit
Critical PGL-1 report and primary-assay assessment (2026-09-21)