PGL-1 is an RNA-binding P-granule scaffold in Caenorhabditis elegans germ cells. Self-association and recruitment of RNA and protein partners help organize germ granules; PGL-1 directly binds the translation initiation factor IFE-1 and supports its granule localization. PGL-1 also promotes FBF-2 recruitment and RNA repression, and its assembly supports WAGO-1-dependent repression of tethered reporter mRNA. Its central dimerization domain also has guanosine-specific single-stranded RNA endonuclease activity in vitro, although the native substrates and physiological role of that catalysis remain unresolved. PGL-1 supports germline proliferation, gametogenesis and fertility, with temperature-sensitive defects and partial redundancy with PGL-3. It also suppresses excessive apoptosis and regulates CED-4 protein levels and SIR-2.1 localization. PGL-1 is a constituent of cytoplasmic germ granules, including perinuclear granules in the adult germline.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003724 RNA helicase activity | IBA GO_REF:0000033 | UNDECIDED | Summary: Inherited RNA helicase activity remains unresolved against the target-specific PGL structural evidence. Reason: The exact Q9TZQ3/PTN002773363 leaf really descends from helicase IBD PTN002774595, without a known helicase-loss node on its path. Two experimentally characterized PGL dimerization domains and the absence of conventional DEAD-box patterns create a specific conflict with its DDX39-like placement. The focused OpenScientist report supports that architecture difference, but overstates it as a direct helicase refutation: its strict control patterns need correction, the structures cover domains rather than full-length protein, and the 2016 experiments assay RNase cleavage, not ATP-driven unwinding. Live GO:0003724 requires ATP-driven unwinding. The reported GAR1 classification is only a 629β728 RGG-tail match, not a verified full-protein reassignment or misgraft. Retain UNDECIDED after completed report review; curator inspection of the actual MSA/sequence placement and a direct unwinding assay remain discriminating follow-ups. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002774595 UNRESOLVED Exact positive descent remains verified. PGL domain structures and the reproduced motif differences raise a concrete alignment/identity question for its DDX39-like placement. Neither the partial GAR1-tail match nor the report establishes a misgraft or a direct negative helicase assay. Supporting Evidence: file:worm/pgl-1/pgl-1-paint-lineage.md This is a real positive ancestry, not an off-clade target or a missing-source failure. PMID:26787882 PGL-1 DD has a novel 13 Ξ±-helix fold that creates a positively charged channel as a homodimer. file:worm/pgl-1/pgl-1-bioinformatics/RESULTS.md PGL-1 lacks all five tested patterns, including versions allowing the actual GLH-1 residues. file:worm/pgl-1/pgl-1-report-assessment.md No direct helicase-negative assay is reported in these Results or Methods. file:worm/pgl-1/pgl-1-hypotheses/pgl-fold-and-inherited-helicase-rna-processing/openscientist.md This would convert the sequence/structure-based helicase refutation into a direct negative result. |
| GO:0003729 mRNA binding | IBA GO_REF:0000033 | ACCEPT | Summary: PGL-1 retains mRNA binding as an inherited RNA-recognition function. Reason: The exact target descends from mRNA-binding IBD PTN002776867. PGL RNA-binding and RNA recruitment to granules are independently established. This term does not require preference for mRNA over every other RNA class; absence of that selectivity is not a reason to replace it with generic RNA binding. The unresolved helicase architecture does not contradict mRNA binding itself. Supporting Evidence: file:worm/pgl-1/pgl-1-paint-lineage.md The target descends from PTN002776867 (mRNA binding), PTN002774595 (RNA helicase), PMID:21402787 PGL proteins autonomously form RNP granules that contain endogenous RNA, PABP, and certain coexpressed C. elegans P-granule components. |
| GO:0000398 mRNA splicing, via spliceosome | IBA GO_REF:0000033 | UNDECIDED | Summary: Inherited mRNA splicing, via spliceosome remains unresolved against the target-specific PGL structural evidence. Reason: The exact target descends from positive spliceosomal-process IBD PTN002776405. Its experimentally characterized PGL scaffold architecture conflicts with the conventional DDX39-like family placement and warrants an MSA/sequence audit, but no spliceosomal contribution has been directly refuted. The focused report acknowledges untested noncatalytic participation, then recommends rejection from absence of target experiments and cytoplasmic localization; those are insufficient grounds to negate an inherited process. The later primary study establishes scaffold-dependent reporter repression, with WAGO-1 required for full repression, rather than testing splicing. That positive post-transcriptional role neither proves nor excludes a spliceosomal role. Retain UNDECIDED for the concrete placement/function conflict after report incorporation, not because an IBA lacks target-specific experimental duplication. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002776405 UNRESOLVED Positive descent is established. The target-domain/DDX39-placement discrepancy is unresolved, but loss of helicase catalysis would not exclude a noncatalytic spliceosomal role. The report supplies no direct negative splicing assay. Supporting Evidence: file:worm/pgl-1/pgl-1-paint-lineage.md This is a real positive ancestry, not an off-clade target or a missing-source failure. PMID:26787882 PGL-1 DD has a novel 13 Ξ±-helix fold that creates a positively charged channel as a homodimer. file:worm/pgl-1/pgl-1-hypotheses/pgl-fold-and-inherited-helicase-rna-processing/openscientist.md Noncatalytic moonlighting is untested, not disproven. file:worm/pgl-1/pgl-1-report-assessment.md The unresolved issue is the alignment and sequence identity supporting this actual placement, not donor number. PMID:33579952 These results also provide direct evidence that granule formation alone is not sufficient for mRNA regulation |
| GO:0006406 mRNA export from nucleus | IBA GO_REF:0000033 | UNDECIDED | Summary: Inherited mRNA export from nucleus remains unresolved against the target-specific PGL structural evidence. Reason: The exact target inherits mRNA export from positive IBD PTN002776405. PGL-specific structural architecture still requires reconciliation with this DDX39-like placement. The focused report does not resolve that alignment/identity issue, and its claim that export work must occur on the inner nuclear face is too restrictive: GO:0006406 covers directed movement to the cytoplasm. P granules receive newly exported transcripts, and full PMID:22991439 discusses their continuity with the pore environment while demonstrating PGL-1-dependent FBF-2 localization and efficient mRNA binding. Those are compatible contextual observations, not a direct PGL-1 export assay; cytoplasmic/perinuclear localization cannot refute export participation. Retain UNDECIDED for the specific unresolved placement and process contribution, assessed independently from helicase activity and without a duplicate provider request. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002776405 UNRESOLVED The target lies below this positive export node. A PGL structural/sequence-placement discrepancy remains, but the partial GAR1 match does not identify a misgraft. Export at the cytoplasmic pore interface remains possible; neither missing target assays nor loss of catalytic helicase activity is a process-level refutation. Supporting Evidence: file:worm/pgl-1/pgl-1-paint-lineage.md This is a real positive ancestry, not an off-clade target or a missing-source failure. PMID:26787882 PGL-1 DD has a novel 13 Ξ±-helix fold that creates a positively charged channel as a homodimer. PMID:22991439 P granules are major sites of RNA export from the nucleus PMID:20223759 newly exported mRNAs are collected prior to their release to the general cytoplasm file:worm/pgl-1/pgl-1-hypotheses/pgl-fold-and-inherited-helicase-rna-processing/openscientist.md Noncatalytic moonlighting is untested, not disproven. file:worm/pgl-1/pgl-1-report-assessment.md These observations do not prove that PGL-1 executes export, but cytoplasmic localization does not refute it. |
| GO:0003723 RNA binding | IEA GO_REF:0000043 | ACCEPT | Summary: RNA binding is a core function of PGL-1 mediated by its RGG repeats. The protein binds RNA to recruit it into P granules and also has ribonuclease activity that requires RNA binding. This annotation is well-supported despite being IEA. Reason: PGL-1 contains RGG repeats that are well-characterized RNA-binding motifs. The protein recruits RNA into P granules and has demonstrated ribonuclease activity, both requiring RNA binding capability. This is a fundamental molecular function of the protein. Supporting Evidence: PMID:21402787 an RGG box for recruiting RNA and RNA-binding proteins |
| GO:0004518 nuclease activity | IEA GO_REF:0000043 | ACCEPT | Summary: The broad nuclease annotation is consistent with directly demonstrated RNA endonuclease activity. Reason: PMID:26787882 establishes guanosine-specific single-stranded RNA endonucleolysis. Nuclease and endonuclease are true broader activities; a more specific retained term does not make the electronic annotation biologically incorrect. Supporting Evidence: PMID:26787882 PGL-1 DD is a guanosine-specific, single-stranded endonuclease |
| GO:0004519 endonuclease activity | IEA GO_REF:0000043 | ACCEPT | Summary: The broad nuclease annotation is consistent with directly demonstrated RNA endonuclease activity. Reason: PMID:26787882 establishes guanosine-specific single-stranded RNA endonucleolysis. Nuclease and endonuclease are true broader activities; a more specific retained term does not make the electronic annotation biologically incorrect. Supporting Evidence: PMID:26787882 PGL-1 DD is a guanosine-specific, single-stranded endonuclease |
| GO:0016787 hydrolase activity | IEA GO_REF:0000043 | ACCEPT | Summary: The assigned overall guanyl-RNase reaction supports broad hydrolase activity. Reason: UniProt explicitly assigns a reaction consuming H2O and producing a 3β²-phosphate RNA fragment. The cyclizing reaction is classified as a lyase by EC and GO, but that classification does not exclude a hydrolytic step in the overall reaction. GO:0046589 is not an ontological child of hydrolase; the broad annotation is instead supported by the curated reaction itself. Primary evidence establishes G-specific cleavage while the exact novel PGL catalytic mechanism remains open. Neither broadness nor lack of a separate product-mechanism assay justifies rejecting the curated chemical assignment. Supporting Evidence: file:worm/pgl-1/pgl-1-uniprot.txt Reaction=[RNA] containing guanosine + H2O PMID:26787882 PGL-1 DD is a guanosine-specific, single-stranded endonuclease |
| GO:0016829 lyase activity | IEA GO_REF:0000043 | ACCEPT | Summary: This annotation is correct. PGL-1 has lyase activity because it generates 2,3-cyclic phosphate intermediates when cleaving RNA, which is characteristic of lyase-type ribonucleases like RNase T1. Reason: Retain the curated EC/keyword mapping at its inferred chemical-reaction scope. Direct biochemical evidence establishes guanosine-specific RNA endonucleolysis, while UniProt assigns the cyclizing RNase reaction. Exact product chemistry and native substrate use are less directly established than the cleavage itself; this annotation does not imply that RNase catalysis is required for granule assembly or fertility. Supporting Evidence: file:worm/pgl-1/pgl-1-uniprot.txt formation of a corresponding 2',3'-cyclic phosphate intermediate PMID:26787882 PGL-1 DD is a guanosine-specific, single-stranded endonuclease |
| GO:0030154 cell differentiation | IEA GO_REF:0000043 | ACCEPT | Summary: PGL-1 contributes to germline cell differentiation and development. Reason: The broad electronic cell-differentiation term is consistent with the experimental germline phenotypes and granule organization role. More specific existing germline terms add detail without refuting this ancestor. Supporting Evidence: PMID:9741628 its primary function is in germline proliferation. |
| GO:0046589 ribonuclease T1 activity | IEA GO_REF:0000003 | ACCEPT | Summary: This annotation is essentially correct. PGL-1 has guanosine-specific ribonuclease activity similar to RNase T1, cleaving RNA after guanosine residues and generating 2,3-cyclic phosphates. The EC number 4.6.1.24 confirms this. The direct biochemical/structural evidence comes from Aoki et al. 2016 (PMID:26787882, IDA), which demonstrated guanosine-specific ssRNA cleavage and identified catalytic residues by mutagenesis. Note that the falcon deep research (focused on 2023-2024 germ-granule literature) could not independently retrieve the underlying enzymology and therefore treated the RNase function as "unverified in this report"; this reflects the corpus accessible to falcon rather than a genuine contradiction, since the primary biochemical paper provides direct catalytic evidence. Recent compartment-mapping literature continues to label PGL-1 a P-granule endoribonuclease. Reason: Retain the curated EC/keyword mapping at its inferred chemical-reaction scope. Direct biochemical evidence establishes guanosine-specific RNA endonucleolysis, while UniProt assigns the cyclizing RNase reaction. Exact product chemistry and native substrate use are less directly established than the cleavage itself; this annotation does not imply that RNase catalysis is required for granule assembly or fertility. Supporting Evidence: file:worm/pgl-1/pgl-1-uniprot.txt formation of a corresponding 2',3'-cyclic phosphate intermediate PMID:26787882 PGL-1 DD is a guanosine-specific, single-stranded endonuclease |
| GO:0048477 oogenesis | IEA GO_REF:0000043 | ACCEPT | Summary: This annotation is correct. PGL-1 is essential for oogenesis in C. elegans. Loss of PGL-1 leads to defective oocyte production and female sterility, especially at elevated temperatures. Reason: PGL-1 is required for correct oogenesis. Mutants show defective oocyte production and hermaphrodites lacking PGL-1 have impaired fertility due to oogenesis defects. This is experimentally validated by multiple studies. Supporting Evidence: file:worm/pgl-1/pgl-1-uniprot.txt required for correct oogenesis PMID:9741628 Elimination of PGL-1 results in defective germ granules and sterility. |
| GO:0005515 protein binding | IPI PMID:11641215 An isoform of eIF4E is a component of germ granules and is r... | REMOVE | Summary: PGL-1 directly interacts with IFE-1 and recruits it to P granules. Reason: Remove the generic protein-binding annotation because it does not describe a specific molecular function. The interaction evidence and source attribution are retained; this curation action does not assert that the reported association is false. The inspected evidence does not justify an informative replacement function for this particular row. Supporting Evidence: PMID:11641215 In vitro PGL-1 interacts directly with IFE-1, but not with the other four isoforms of eIF4E. |
| GO:0005515 protein binding | IPI PMID:14704431 A map of the interactome network of the metazoan C. elegans. | UNDECIDED | Summary: The experimentally curated interaction from the worm Y2H interactome is retained. Reason: The curated interaction is not contradicted, but the accessible evidence does not expose the target-specific assay needed to choose a more informative molecular function. Leave this row unresolved pending source inspection; generic protein binding is not accepted as a functional synthesis, and lack of accessible assay detail is not evidence that the interaction is false. Supporting Evidence: PMID:14704431 more than 4000 interactions were identified from high-throughput, yeast two-hybrid (HT=Y2H) screens. |
| GO:0004521 RNA endonuclease activity | IDA PMID:26787882 PGL germ granule assembly protein is a base-specific, single... | ACCEPT | Summary: PGL-1 has directly demonstrated guanosine-specific ssRNA endonuclease activity. Reason: The primary study establishes cleavage by the PGL dimerization domain. Native RNA substrates and the physiological contribution of this activity remain unresolved; RNase-defective mutants can retain the tested in vivo functions. The molecular activity is supported independently of those downstream process questions. Supporting Evidence: PMID:26787882 PGL-1 DD is a guanosine-specific, single-stranded endonuclease PMID:26787882 that enzymatic activity is dispensable in vivo. |
| GO:0042802 identical protein binding | IPI PMID:26787882 PGL germ granule assembly protein is a base-specific, single... | ACCEPT | Summary: Excellent annotation. PGL-1 homodimerization is structurally and functionally characterized. The dimerization domain is essential for P granule assembly and the protein forms homodimers as building blocks. Reason: Crystal structure and biochemical studies confirm PGL-1 forms homodimers through its dimerization domain. This self-association is fundamental to P granule assembly and represents a core molecular function. Supporting Evidence: PMID:26787882 PGL-1 DD has a novel 13 Ξ±-helix fold that creates a positively charged channel as a homodimer. file:worm/pgl-1/pgl-1-uniprot.txt Homodimer |
| GO:0005515 protein binding | IPI PMID:31283754 The demethylase NMAD-1 regulates DNA replication and repair ... | UNDECIDED | Summary: The NMAD-1-associated protein-interaction evidence is retained. Reason: The curated interaction is not contradicted, but the accessible evidence does not expose the target-specific assay needed to choose a more informative molecular function. Leave this row unresolved pending source inspection; generic protein binding is not accepted as a functional synthesis, and lack of accessible assay detail is not evidence that the interaction is false. Supporting Evidence: file:worm/pgl-1/pgl-1-uniprot.txt Interacts with nmad-1 PMID:31283754 we used immunoprecipitation and mass spectrometry to identify NMAD-1 binding proteins. |
| GO:0043186 P granule | IDA PMID:28182654 ELLI-1, a novel germline protein, modulates RNAi activity an... | ACCEPT | Summary: Excellent cellular component annotation. PGL-1 is a core structural component of P granules, experimentally validated by direct observation. Reason: PGL-1 is a defining component of P granules. It localizes to these germline-specific cytoplasmic granules throughout development and is essential for their assembly. This is fundamental to its cellular localization. Supporting Evidence: PMID:28182654 ELLI-1, a novel germline protein, modulates RNAi activity and P-granule accumulation in Caenorhabditis elegans. file:worm/pgl-1/pgl-1-uniprot.txt Localizes to P granules in germline precursor cells |
| GO:0043186 P granule | IDA PMID:19361491 The C. elegans sex determination gene laf-1 encodes a putati... | ACCEPT | Summary: PGL-1 is the P-granule colocalization marker in the LAF-1 study. Reason: The primary abstract explicitly reports LAF-1 colocalization with PGL-1 in germline precursor granules. This supports PGL-1 location, not transfer of LAF-1 helicase activity. Supporting Evidence: PMID:19361491 LAF-1 is predominantly, if not exclusively, cytoplasmic and colocalizes with PGL-1 in P granules of germline precursor cells. |
| GO:0043186 P granule | IDA PMID:26015579 The disordered P granule protein LAF-1 drives phase separati... | ACCEPT | Summary: The PGL-1 granule localization observation is retained from the LAF-1 phase-separation study. Reason: WormBase curates an IDA location observation from this study. The paper primarily characterizes LAF-1, so its phase-separation mechanism must not be reassigned to PGL-1 merely because PGL-1 marks the granules. Independent PGL-1 localization and scaffold studies corroborate the location. Supporting Evidence: PMID:9741628 PGL-1 is a predicted RNA-binding protein that is present on germ granules at all stages of development. |
| GO:0003723 RNA binding | ISS PMID:9741628 PGL-1, a predicted RNA-binding component of germ granules, i... | ACCEPT | Summary: Early prediction of RNA binding based on RGG repeats, later confirmed experimentally. This annotation is correct and represents a core molecular function. Reason: The initial sequence-based prediction of RNA binding through RGG repeats has been validated by subsequent experimental work showing PGL-1 binds and cleaves RNA. This is a fundamental molecular function. Supporting Evidence: PMID:21402787 an RGG box for recruiting RNA and RNA-binding proteins |
| GO:0007276 gamete generation | IMP PMID:9741628 PGL-1, a predicted RNA-binding component of germ granules, i... | ACCEPT | Summary: Excellent annotation. PGL-1 mutants are sterile due to defects in both oogenesis and spermatogenesis, demonstrating essential role in gamete generation. Reason: Genetic evidence clearly shows PGL-1 is essential for gamete generation. Mutants fail to produce functional oocytes and sperm, resulting in sterility. This is a core biological function. Supporting Evidence: PMID:9741628 Elimination of PGL-1 results in defective germ granules and sterility. file:worm/pgl-1/pgl-1-deep-research.md mutant males have defective sperm production and mutant hermaphrodites have faulty oocyte production PMID:15238518 The PGL family proteins associate with germ granules and function redundantly in Caenorhabditis elegans germline development. |
| GO:0022414 reproductive process | IMP PMID:9741628 PGL-1, a predicted RNA-binding component of germ granules, i... | ACCEPT | Summary: PGL-1 contributes to reproductive development through germline proliferation and gametogenesis. Reason: The source IMP annotation is biologically consistent with the primary fertility and germline defects. Being broader than gamete generation or oogenesis does not make it non-core or erroneous. Supporting Evidence: PMID:9741628 Elimination of PGL-1 results in defective germ granules and sterility. |
| GO:0030719 P granule organization | IMP PMID:9741628 PGL-1, a predicted RNA-binding component of germ granules, i... | ACCEPT | Summary: Excellent annotation for a core function. PGL-1 is essential for P granule assembly and organization, acting as a scaffold protein that nucleates granule formation. Reason: PGL-1 is a fundamental P granule scaffold protein. Loss of PGL-1 results in defective or absent P granules. The protein self-associates and recruits other components to form organized P granules. This is a defining biological function. Supporting Evidence: PMID:21402787 an RGG box for recruiting RNA and RNA-binding proteins PMID:9741628 Elimination of PGL-1 results in defective germ granules and sterility. |
| GO:0042078 germ-line stem cell division | IMP PMID:9741628 PGL-1, a predicted RNA-binding component of germ granules, i... | ACCEPT | Summary: PGL-1 is required for germline proliferation. Mutants show germline proliferation defects with insufficient mitotic germ cells, supporting this annotation. Reason: PGL-1 mutants exhibit early germ cell proliferation arrest, failing to maintain the population of mitotically dividing germ cells. This demonstrates a requirement for germline stem cell division. Supporting Evidence: PMID:9741628 its primary function is in germline proliferation. file:worm/pgl-1/pgl-1-uniprot.txt population of proliferating germ cells |
| GO:0043186 P granule | IDA PMID:9741628 PGL-1, a predicted RNA-binding component of germ granules, i... | ACCEPT | Summary: Original demonstration of PGL-1 localization to P granules. This foundational observation established PGL-1 as a P granule component. Reason: This is the original paper identifying PGL-1 as a P granule component present at all developmental stages. This fundamental localization is essential to understanding PGL-1 function. Supporting Evidence: PMID:9741628 PGL-1 is a predicted RNA-binding protein that is present on germ granules at all stages of development. file:worm/pgl-1/pgl-1-deep-research-falcon.md PGL-1 localizes to **perinuclear P granules** in the adult germline, a positioning that connects germ granules to nuclear pores and nascent transcripts. |
| GO:0048477 oogenesis | IMP PMID:9741628 PGL-1, a predicted RNA-binding component of germ granules, i... | ACCEPT | Summary: Well-supported annotation. PGL-1 is required for oogenesis, with mutants showing defective or absent oocyte production. Reason: Genetic evidence demonstrates PGL-1 is essential for oogenesis. Mutant hermaphrodites have defective oocyte production, particularly at elevated temperatures, confirming this biological role. Supporting Evidence: file:worm/pgl-1/pgl-1-uniprot.txt required for correct oogenesis PMID:9741628 Elimination of PGL-1 results in defective germ granules and sterility. |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:26598553 Loss of PGL-1 and PGL-3, members of a family of constitutive... | NEW | Summary: PGL-1 negatively regulates apoptosis, with evidence for control of CED-4 protein expression. Reason: Retain this existing authored IMP proposal based on germline loss-of-function, ectopic-expression sufficiency and PGL-1-dependent changes in CED-4 reporter protein despite unchanged ced-4 RNA in the somatic model. PGL-1 therefore supplies regulatory work rather than merely being necessary for cell viability. Exact molecular effectors remain unresolved: no direct PGL-1/SIR-2.1 sequestration complex or direct ced-4 RNA interaction is asserted. QuickGO ancestry checked on 2026-09-20 has no parent/child redundancy with the existing process rows. Supporting Evidence: PMID:26598553 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. PMID:27650246 CED-4::GFP expression was recovered to a higher level by RNAi depletion of pgl-1 in hpl-2-mutant embryos compared to mock RNAi-treated hpl-2-mutant embryos |
Loading supporting contentβ¦
Download this section (compressed HTML)Q: Can a PAINT curator reconcile the exact Q9TZQ3 sequence/MSA beneath positive helicase PTN002774595 and splicing/export PTN002776405 with both PGL dimerization domains? The report is incorporated but did not establish a misgraft; its GAR1 match covers only the RGG tail. Which of the three inherited capacities is supported independently by direct full-length unwinding or target-resolved RNA-processing/export evidence?
Q: Which physiological RNAs are cleaved by PGL-1, what are the reaction products, and does it catalyse a water-dependent hydrolytic step as well as the assigned cyclizing reaction?
Q: How does PGL-1 lower CED-4 protein and alter SIR-2.1 localization, and is either effect mediated by direct RNA recognition or a demonstrable sequestration complex?
Experiment: RNA-seq of PGL-1 immunoprecipitates to identify direct RNA targets and analysis of RNA cleavage sites
Hypothesis: PGL-1 binds and cleaves specific germline mRNAs involved in cell fate determination and translational control
Type: Biochemical RNA-seq analysis
Experiment: Systematic mutagenesis of PGL-1 ribonuclease active site and dimerization domains to separate enzymatic and scaffolding functions
Hypothesis: PGL-1's ribonuclease activity and scaffolding function are separable and have distinct roles in germline development
Type: Structure-function mutagenesis
Experiment: Time-lapse microscopy of P granule dynamics and PGL-1 behavior in wild-type vs mutant backgrounds at permissive vs restrictive temperatures
Hypothesis: Temperature affects PGL-1 stability, P granule assembly dynamics, or protein interactions critical for germline function
Type: Live cell imaging at different temperatures
Experiment: Single-cell analysis of SIR-2.1, CED-4, and other apoptosis factors in PGL-1 mutant germ cells to map the apoptosis regulatory network
Hypothesis: PGL-1 coordinates a specific subcellular organization that spatially regulates pro- and anti-apoptotic factors
Type: Single-cell proteomics of apoptosis regulation
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)