cgh-1

Existing Annotations Review

GO Term	Evidence	Action	Reason
GO:0000932 P-body	IBA GO_REF:0000033	ACCEPT	Summary: CGH-1 localization to P-bodies is well-supported by phylogenetic inference. The yeast ortholog Dhh1p is a core component of P-bodies, and direct experimental evidence in C. elegans confirms CGH-1 localizes to P-bodies (PMID:16207815, PMID:24367695). Reason: IBA annotation is consistent with experimental IDA evidence in C. elegans showing CGH-1 localizes to P-bodies. P-body localization is a conserved feature of the DDX6/Dhh1p family across eukaryotes. Supporting Evidence: PMID:18692039 P-bodies contain complexes that inhibit translation and stimulate mRNA deadenylation, decapping, and decay PMID:24367695 PAB-1 colocalizes with P-body components, CAR-1 and CGH-1 file:worm/cgh-1/cgh-1-deep-research-falcon.md Somatic P-bodies that are PATR-1 (Pat1)–dependent and linked to decapping-mediated turnover (boag2008protectionofspecific pages 1-2, boag2008protectionofspecific pages 4-5).
GO:0003729 mRNA binding	IBA GO_REF:0000033	ACCEPT	Summary: CGH-1 is a DEAD-box RNA helicase that functions in mRNA metabolism. Its association with mRNA-containing complexes is well-established, and mRNA binding is a conserved function of DDX6 family helicases. Reason: mRNA binding is expected for a DEAD-box helicase that functions in mRNA metabolism and localizes to mRNA-containing granules. The IBA inference from orthologs including yeast Dhh1 and plant homologs is phylogenetically sound. Supporting Evidence: PMID:16247027 CAR-1 is a component of an RNase-sensitive, multiprotein complex of conserved RNA-binding proteins file:worm/cgh-1/cgh-1-deep-research-falcon.md Maternal mRNA association in oogenesis: 92% of CGH-1–associated mRNAs are expressed mainly in the gonad and 85% are classified as maternal (boag2008protectionofspecific pages 7-8).
GO:0017148 negative regulation of translation	IBA GO_REF:0000033	ACCEPT	Summary: Translational repression is a core function of CGH-1. Direct experimental evidence (IMP from PMID:18692039) supports this annotation in C. elegans. The IBA annotation is redundant with experimental evidence but correctly captures this conserved function. Reason: IBA is consistent with direct experimental evidence from PMID:18692039 showing CGH-1 functions in negative regulation of translation in C. elegans. This is a conserved function of DDX6/Dhh1p family members. Supporting Evidence: PMID:18692039 P-bodies contain complexes that inhibit translation and stimulate mRNA deadenylation, decapping, and decay file:worm/cgh-1/cgh-1-deep-research-falcon.md CGH-1 helps route mRNAs between translation, storage, and decay depending on developmental context.
GO:0010494 cytoplasmic stress granule	IBA GO_REF:0000033	ACCEPT	Summary: CGH-1 localization to stress granules is supported by both IBA inference and direct experimental evidence (IDA from PMID:24844228). CGH-1 co-localizes with VBH-1 in stress-induced granules. Reason: The IBA annotation is consistent with experimental IDA evidence showing CGH-1 localizes to cytoplasmic stress granules. This is a conserved feature of DDX6 family helicases. Supporting Evidence: PMID:24844228 VBH-1 colocalized with CGH-1 in the gonad core granules and large P granules observed during heat shock
GO:0033962 P-body assembly	IBA GO_REF:0000033	ACCEPT	Summary: CGH-1 role in P-body assembly is supported by both IBA inference and direct experimental evidence (IMP from PMID:25061667). The yeast ortholog Dhh1p is essential for P-body assembly. Reason: The IBA annotation is consistent with experimental IMP evidence showing CGH-1 is required for P-body assembly in C. elegans. This is a conserved function of the DDX6/Dhh1p family. Supporting Evidence: PMID:25061667 Accumulation of DCAP-1-containing granules under heat-shock is rapid, reversible and sensitive to cgh-1(RNAi) file:worm/cgh-1/cgh-1-deep-research-falcon.md Condensate dependence: loss of patr-1 causes ~12-fold fewer somatic CGH-1 foci by the ~100-cell stage, supporting PATR-1 dependence of somatic P-body CGH-1 localization (boag2008protectionofspecific pages 4-5).
GO:0034063 stress granule assembly	IBA GO_REF:0000033	ACCEPT	Summary: CGH-1 involvement in stress granule assembly is inferred from phylogenetic analysis. While CGH-1 localizes to stress granules (PMID:24844228), direct evidence for its role in assembly is less clear in C. elegans than for P-bodies. Reason: The IBA annotation from ortholog evidence is reasonable given CGH-1 localizes to stress granules and the DDX6 family is broadly involved in stress granule dynamics. CGH-1 co-localization with stress granule markers during heat shock supports this. Supporting Evidence: PMID:24844228 VBH-1 colocalized with CGH-1 in the gonad core granules and large P granules observed during heat shock
GO:0000166 nucleotide binding	IEA GO_REF:0000043	ACCEPT	Summary: CGH-1 contains a DEAD-box helicase domain with conserved Walker A motif for nucleotide binding. This is an accurate but very general annotation. Reason: Correct but redundant with more specific ATP binding annotation. The protein contains conserved nucleotide binding motifs as expected for a DEAD-box helicase. The annotation is based on UniProtKB keyword mapping and is accurate.
GO:0003676 nucleic acid binding	IEA GO_REF:0000002	ACCEPT	Summary: CGH-1 is an RNA helicase with demonstrated RNA binding function. This term is accurate but overly general given the more specific mRNA binding annotation. Reason: The InterPro domain-based annotation is correct - DEAD box helicases bind nucleic acids. This is redundant with but not contradicted by the more specific mRNA binding annotation.
GO:0003723 RNA binding	IEA GO_REF:0000043	ACCEPT	Summary: CGH-1 is an RNA helicase that binds RNA as part of its catalytic function and in forming ribonucleoprotein complexes with CAR-1, PAB-1, and other factors. Reason: RNA binding is an essential activity for an RNA helicase. The UniProtKB keyword mapping correctly captures this core molecular function. Supporting Evidence: PMID:16247027 CAR-1 associates with the essential RNA helicase CGH-1 file:worm/cgh-1/cgh-1-deep-research-falcon.md CGH-1 has ATPase activity that can be robustly stimulated by the MIF4G domain of NTL-1a in the presence of poly(U) RNA and ATP, consistent with conserved activation of DDX6-family ATPases by MIF4G-containing partners (zhang2021insightintothe pages 5-7, zhang2021insightintothe pages 4-5). This supports RNA as the relevant substrate class
GO:0003724 RNA helicase activity	IEA GO_REF:0000120	ACCEPT	Summary: CGH-1 is a DEAD-box RNA helicase with conserved catalytic domains. RNA helicase activity is directly supported by ISS annotation (PMID:11546739) based on sequence similarity to characterized helicases. Reason: This is a core molecular function for CGH-1. The annotation is well-supported by domain architecture (DEAD box, helicase C-terminal domain) and sequence similarity to characterized RNA helicases. Supporting Evidence: PMID:11546739 cgh-1, a conserved predicted RNA helicase required for gametogenesis file:worm/cgh-1/cgh-1-deep-research-falcon.md CGH-1 is an ATP-dependent RNA helicase/ATPase (EC 3.6.4.13 in UniProt), but like many DEAD-box proteins, its primary biochemical role is understood as ATP-driven remodeling of RNA-containing complexes rather than sequence-specific catalysis of a small-molecule reaction.
GO:0004386 helicase activity	IEA GO_REF:0000043	ACCEPT	Summary: CGH-1 contains DEAD-box helicase domains. This is a correct but general annotation that is subsumed by the more specific RNA helicase activity annotation. Reason: The UniProtKB keyword mapping is accurate. The term is general but not incorrect. RNA helicase activity is a more specific child term.
GO:0005524 ATP binding	IEA GO_REF:0000120	ACCEPT	Summary: CGH-1 contains a conserved Walker A motif (positions 87-94 per UniProt) for ATP binding. ATP binding is essential for DEAD-box helicase function. Reason: ATP binding is a core molecular function for DEAD-box helicases and is structurally supported by the presence of the conserved ATP-binding helicase domain.
GO:0005737 cytoplasm	IEA GO_REF:0000044	ACCEPT	Summary: CGH-1 is cytoplasmic, localizing to cytoplasmic granules including P granules and P-bodies. This is confirmed by experimental evidence (PMID:11546739). Reason: Cytoplasmic localization is accurate but general. More specific localizations (P granule, P-body, stress granule) are also annotated. Supporting Evidence: PMID:11546739 CGH-1 is expressed specifically in the germline and early embryo, and is localized to P granules and other possible mRNA-protein particles
GO:0006915 apoptotic process	IEA GO_REF:0000043	MODIFY	Summary: CGH-1 is involved in regulating apoptosis, specifically protecting against physiological germline apoptosis. However, this term is too general and the relationship is regulatory rather than being a core component of apoptosis. Reason: The term is too general. CGH-1 does not execute apoptosis; rather it negatively regulates physiological germline apoptosis (PMID:11546739). The more specific annotation GO:0043066 (negative regulation of apoptotic process) is already present and more accurate. Proposed replacements: negative regulation of apoptotic process Supporting Evidence: PMID:11546739 It is also needed to prevent the physiological germline apoptosis mechanism killing essentially all developing oocytes, making lack of cgh-1 function the first stimulus identified that can trigger this mechanism
GO:0007283 spermatogenesis	IEA GO_REF:0000043	ACCEPT	Summary: CGH-1 is required for sperm function as demonstrated by experimental evidence (PMID:11546739). The UniProtKB keyword-based annotation is accurate. Reason: The annotation is supported by experimental evidence from PMID:11546739 showing cgh-1 is required for sperm function. This is captured by the gamete generation IMP annotation but spermatogenesis specifically is accurate. Supporting Evidence: PMID:11546739 cgh-1 is required for oocyte and sperm function
GO:0016787 hydrolase activity	IEA GO_REF:0000043	ACCEPT	Summary: CGH-1 has ATP hydrolysis activity as part of its helicase function. This is a very general term but is accurate. Reason: ATP hydrolysis is inherent to DEAD-box helicase function. This annotation is correct but general; the more specific ATP hydrolysis activity is also annotated.
GO:0016887 ATP hydrolysis activity	IEA GO_REF:0000116	ACCEPT	Summary: CGH-1 is a DEAD-box helicase that couples ATP hydrolysis to RNA unwinding. This is a core catalytic activity for the protein. Reason: ATP hydrolysis activity is essential for DEAD-box helicase function. The Rhea-based annotation correctly captures this enzymatic activity. Supporting Evidence: file:worm/cgh-1/cgh-1-deep-research-falcon.md Direct worm biochemical evidence indicates CGH-1 has ATPase activity that can be robustly stimulated by the MIF4G domain of NTL-1a in the presence of poly(U) RNA and ATP
GO:0017148 negative regulation of translation	IEA GO_REF:0000117	ACCEPT	Summary: CGH-1 functions in translational repression, consistent with its localization to P-bodies and its role in mRNA regulation. This is also supported by experimental IMP evidence (PMID:18692039). Reason: The ARBA machine learning annotation is consistent with experimental evidence showing CGH-1 negatively regulates translation. This is a core function of P-body components. Supporting Evidence: PMID:18692039 P-bodies contain complexes that inhibit translation and stimulate mRNA deadenylation, decapping, and decay
GO:0030154 cell differentiation	IEA GO_REF:0000043	KEEP AS NON CORE	Summary: CGH-1 is involved in germ cell development and gametogenesis, which involves cell differentiation. However, this term is very general. Reason: While CGH-1 is involved in germ cell development, "cell differentiation" is very broad. The more specific annotations for gametogenesis, oogenesis, and spermatogenesis better capture CGH-1's role. This annotation is not incorrect but represents a secondary consequence of its primary functions.
GO:0033962 P-body assembly	IEA GO_REF:0000117	ACCEPT	Summary: CGH-1 role in P-body assembly is well-supported by experimental IMP evidence (PMID:25061667) showing cgh-1(RNAi) reduces DCAP-1 granule formation. Reason: The ARBA annotation is consistent with experimental evidence. P-body assembly is a conserved function of DDX6/Dhh1p family helicases. Supporting Evidence: PMID:25061667 Accumulation of DCAP-1-containing granules under heat-shock is rapid, reversible and sensitive to cgh-1(RNAi)
GO:0043186 P granule	IEA GO_REF:0000117	ACCEPT	Summary: CGH-1 localization to P granules is very well-established by multiple IDA annotations (PMID:11546739, PMID:24367695). This is a core localization. Reason: P granule localization is a key feature of CGH-1, supported by extensive experimental evidence including the original characterization paper. Supporting Evidence: PMID:11546739 CGH-1 is expressed specifically in the germline and early embryo, and is localized to P granules and other possible mRNA-protein particles
GO:0048477 oogenesis	IEA GO_REF:0000043	ACCEPT	Summary: CGH-1 is required for oocyte function as demonstrated experimentally (PMID:11546739). The UniProtKB keyword-based annotation is accurate. Reason: The annotation is supported by experimental evidence showing cgh-1 is required for oocyte function and for protection from germline apoptosis during oogenesis. Supporting Evidence: PMID:11546739 cgh-1 is required for oocyte and sperm function
GO:0005515 protein binding	IPI PMID:12445390 Integrating interactome, phenome, and transcriptome mapping ...	MARK AS OVER ANNOTATED	Summary: This annotation indicates CGH-1 binds to EDC-3 (Q21740) based on protein interaction data. However, "protein binding" is uninformative. Reason: While CGH-1 does interact with other proteins, "protein binding" provides no information about the biological context or specificity of these interactions. The specific interactions with CAR-1, PAB-1, OMA-1 are more informative. Supporting Evidence: PMID:12445390 Integrating interactome, phenome, and transcriptome mapping data for the C.
GO:0005515 protein binding	IPI PMID:14704431 A map of the interactome network of the metazoan C. elegans.	MARK AS OVER ANNOTATED	Summary: Large-scale protein interaction mapping study. "Protein binding" is uninformative as a molecular function annotation. Reason: While the interaction data may be valid, "protein binding" as a GO term provides no functional insight. More specific annotations for the actual binding partners and biological context would be more useful. Supporting Evidence: PMID:14704431 Jan 2. A map of the interactome network of the metazoan C.
GO:0005515 protein binding	IPI PMID:19123269 Empirically controlled mapping of the Caenorhabditis elegans...	MARK AS OVER ANNOTATED	Summary: Protein interaction study with EDC-3 as the binding partner. "Protein binding" is uninformative. Reason: "Protein binding" provides no functional information. The specific interaction with EDC-3 (a decapping activator) is biologically meaningful in the context of P-body function, but this is not captured by the GO term. Supporting Evidence: PMID:19123269 Empirically controlled mapping of the Caenorhabditis elegans protein-protein interactome network.
GO:0035770 ribonucleoprotein granule	IDA PMID:25261697 Translational control of the oogenic program by components o...	ACCEPT	Summary: CGH-1 is part of OMA ribonucleoprotein particles, which are involved in translational control during oogenesis. This is direct experimental evidence. Reason: The IDA annotation correctly captures CGH-1's localization to ribonucleoprotein granules. CGH-1 associates with OMA-1 in an RNA-dependent manner in oocyte RNPs. Supporting Evidence: PMID:25261697 OMA-1 is a component of oocyte RNPs file:worm/cgh-1/cgh-1-deep-research-falcon.md During oogenesis, CGH-1 forms large RNP particles (“storage bodies”) in oocytes and colocalizes with CAR-1-containing foci; these particles are proposed to store maternal mRNAs in a translationally regulated state (boag2008protectionofspecific pages 4-5, boag2008protectionofspecific pages 7-8).
GO:0005515 protein binding	IPI PMID:25261697 Translational control of the oogenic program by components o...	MARK AS OVER ANNOTATED	Summary: CGH-1 interacts with OMA-1 (G5EC86) as shown by co-purification studies. The interaction is RNA-dependent. "Protein binding" is uninformative. Reason: The interaction with OMA-1 is biologically meaningful for understanding CGH-1's role in translational control during oogenesis, but "protein binding" does not capture this. The more informative annotation would describe the complex formation. Supporting Evidence: PMID:25261697 Sep 26. Translational control of the oogenic program by components of OMA ribonucleoprotein particles in Caenorhabditis elegans.
GO:0000932 P-body	IDA PMID:24367695 PAB-1, a Caenorhabditis elegans poly(A)-binding protein, reg...	ACCEPT	Summary: Direct experimental evidence showing CGH-1 localizes to P-bodies. CGH-1 colocalizes with PAB-1 and CAR-1 in P-body structures. Reason: Strong IDA evidence for P-body localization. This is consistent with CGH-1's role in mRNA metabolism and is a conserved feature of DDX6 family helicases. Supporting Evidence: PMID:24367695 PAB-1 colocalizes with P-body components, CAR-1 and CGH-1, in embryos and adult gonads
GO:0016071 mRNA metabolic process	IMP PMID:24367695 PAB-1, a Caenorhabditis elegans poly(A)-binding protein, reg...	ACCEPT	Summary: CGH-1 mutants affect mRNA levels of germline genes. CGH-1 functions with PAB-1 and CAR-1 in regulating germline mRNA metabolism. Reason: Experimental evidence demonstrates CGH-1's role in mRNA metabolism. The cgh-1 mutant shows altered mRNA levels for germline-enriched genes. Supporting Evidence: PMID:24367695 Although the mRNA level of msp-152 was increased in cgh-1 mutant, it was also significantly reduced by pab-1 RNAi file:worm/cgh-1/cgh-1-deep-research-falcon.md A central experimentally supported CGH-1 function in C. elegans is protecting specific maternal mRNAs during oogenesis. CGH-1 forms PATR-1–independent storage bodies and associates with translational regulators and a specific set of maternal transcripts, preventing their degradation (boag2008protectionofspecific pages 1-2).
GO:0043186 P granule	IDA PMID:24367695 PAB-1, a Caenorhabditis elegans poly(A)-binding protein, reg...	ACCEPT	Summary: Direct experimental evidence confirming CGH-1 localization to P granules. This is consistent with multiple other studies. Reason: P granule localization is a core feature of CGH-1, demonstrated by multiple independent studies using immunofluorescence. Supporting Evidence: PMID:24367695 PAB-1 localizes to P granules and the cytoplasm in the germline
GO:0008340 determination of adult lifespan	IMP PMID:25061667 Diverse functions of mRNA metabolism factors in stress defen...	KEEP AS NON CORE	Summary: cgh-1(RNAi) affects worm lifespan. P-body components including CGH-1 influence aging through their roles in mRNA metabolism and stress response. Reason: While experimental evidence shows cgh-1 affects lifespan, this is likely a downstream consequence of its roles in mRNA metabolism and stress response rather than a direct/core function. Many genes affect lifespan indirectly. Supporting Evidence: PMID:25061667 PB components are important for normal lifespan and stress response
GO:0033962 P-body assembly	IMP PMID:25061667 Diverse functions of mRNA metabolism factors in stress defen...	ACCEPT	Summary: cgh-1(RNAi) reduces accumulation of DCAP-1-containing P-body granules, demonstrating CGH-1 is required for P-body assembly. Reason: Strong experimental evidence that CGH-1 is required for P-body assembly under stress conditions. This is a core function of DDX6/Dhh1p family helicases. Supporting Evidence: PMID:25061667 Accumulation of DCAP-1-containing granules under heat-shock is rapid, reversible and sensitive to cgh-1(RNAi)
GO:1990904 ribonucleoprotein complex	IDA PMID:16247027 A complex containing the Sm protein CAR-1 and the RNA helica...	ACCEPT	Summary: CGH-1 is part of an RNA-dependent ribonucleoprotein complex with CAR-1. This complex is required for embryonic cytokinesis. Reason: Direct experimental evidence showing CGH-1 co-purifies with CAR-1 in an RNA-dependent complex. The RNP complex function is central to CGH-1's biology. Supporting Evidence: PMID:16247027 CAR-1 is a component of an RNase-sensitive, multiprotein complex of conserved RNA-binding proteins file:worm/cgh-1/cgh-1-deep-research-falcon.md These interactions place CGH-1 in the canonical P-body/decapping and translational repression network and provide a molecular basis for context-dependent assembly of distinct CGH-1 RNP bodies (zhang2021insightintothe pages 4-5, boag2008protectionofspecific pages 1-2).
GO:0010494 cytoplasmic stress granule	IDA PMID:24844228 The DEAD Box RNA helicase VBH-1 is a new player in the stres...	ACCEPT	Summary: CGH-1 localizes to stress-induced granules in gonads and embryos, co-localizing with VBH-1 during heat shock. Reason: Direct experimental evidence showing CGH-1 localization to stress granules during heat shock. This is consistent with stress granule localization of DDX6 family members in other organisms. Supporting Evidence: PMID:24844228 VBH-1 colocalized with CGH-1 in the gonad core granules and large P granules observed during heat shock
GO:0043186 P granule	IDA PMID:11546739 cgh-1, a conserved predicted RNA helicase required for gamet...	ACCEPT	Summary: The original characterization paper showing CGH-1 localizes to P granules. This is foundational evidence for CGH-1's subcellular localization. Reason: Primary experimental evidence from the paper that first characterized CGH-1 function and localization. P granule localization is a core feature. Supporting Evidence: PMID:11546739 CGH-1 is expressed specifically in the germline and early embryo, and is localized to P granules and other possible mRNA-protein particles file:worm/cgh-1/cgh-1-deep-research-falcon.md Recent imaging and spatial mapping demonstrate that CGH-1 marks perinuclear P-body condensates positioned on the cytoplasmic side of P granules.
GO:0017148 negative regulation of translation	IMP PMID:18692039 Processing bodies and germ granules are distinct RNA granule...	ACCEPT	Summary: Experimental evidence demonstrating CGH-1 functions in translational repression. P-bodies containing CGH-1 inhibit translation of maternal mRNAs. Reason: Direct experimental evidence for CGH-1's role in translational repression. This is a core function of the DDX6/Dhh1p family and consistent with P-body component function. Supporting Evidence: PMID:18692039 P-bodies contain complexes that inhibit translation and stimulate mRNA deadenylation, decapping, and decay file:worm/cgh-1/cgh-1-deep-research-falcon.md In somatic tissues, CGH-1 functions within PATR-1–dependent P-bodies implicated in mRNA decapping and decapping-mediated decay pathways (boag2008protectionofspecific pages 1-2). During oogenesis, CGH-1 instead promotes protection/storage of a defined subset of maternal mRNAs (boag2008protectionofspecific pages 1-2, boag2008protectionofspecific pages 7-8).
GO:0005515 protein binding	IPI PMID:19269369 nhl-2 Modulates microRNA activity in Caenorhabditis elegans.	MARK AS OVER ANNOTATED	Summary: CGH-1 interacts with NHL-2, a microRNA pathway modulator. However, "protein binding" is uninformative. Reason: The interaction with NHL-2 is potentially interesting for understanding CGH-1's role in post-transcriptional regulation, but "protein binding" as a GO term provides no functional insight. Supporting Evidence: PMID:19269369 nhl-2 Modulates microRNA activity in Caenorhabditis elegans.
GO:0000932 P-body	IDA PMID:16207815 Caenorhabditis elegans decapping proteins localization and f...	ACCEPT	Summary: CGH-1 localization to P-bodies demonstrated in the context of decapping protein localization studies. Reason: Direct experimental evidence for P-body localization. Consistent with multiple other studies and the conserved function of DDX6 family proteins. Supporting Evidence: PMID:16207815 Dcp2 is localized to P-granules
GO:0003724 RNA helicase activity	ISS PMID:11546739 cgh-1, a conserved predicted RNA helicase required for gamet...	ACCEPT	Summary: RNA helicase activity inferred from sequence similarity to characterized DEAD-box RNA helicases. CGH-1 contains conserved DEAD box and helicase domains. Reason: The ISS annotation is well-founded given the high conservation of DEAD-box helicase domains and the functional characterization of orthologs like Dhh1p. Crystal structures of CGH-1 domains (PDB:7DTJ, 7DTK) confirm the helicase fold. Supporting Evidence: PMID:11546739 cgh-1, a conserved predicted RNA helicase required for gametogenesis
GO:0007276 gamete generation	IMP PMID:11546739 cgh-1, a conserved predicted RNA helicase required for gamet...	ACCEPT	Summary: cgh-1 mutants show defects in both oocyte and sperm function. CGH-1 is essential for gametogenesis in both sexes. Reason: Primary experimental evidence demonstrating CGH-1 is required for gamete generation. This is a core biological function of the gene. Supporting Evidence: PMID:11546739 cgh-1 is required for oocyte and sperm function
GO:0016071 mRNA metabolic process	TAS PMID:11546739 cgh-1, a conserved predicted RNA helicase required for gamet...	ACCEPT	Summary: CGH-1 functions in mRNA metabolism based on its localization to mRNA-containing granules and its homology to known mRNA metabolism factors. Reason: The TAS annotation is supported by the paper's discussion of CGH-1's role in mRNA regulation during gametogenesis and its localization to P granules. Supporting Evidence: PMID:11546739 CGH-1 is expressed specifically in the germline and early embryo, and is localized to P granules and other possible mRNA-protein particles
GO:0043066 negative regulation of apoptotic process	IMP PMID:11546739 cgh-1, a conserved predicted RNA helicase required for gamet...	ACCEPT	Summary: Loss of cgh-1 causes excessive germline apoptosis, demonstrating CGH-1 normally protects developing oocytes from physiological germline apoptosis. This was the first identified trigger of excessive germline apoptosis. Reason: This is a defining feature of CGH-1 function discovered in the original characterization paper. CGH-1 is required to prevent the germline apoptosis mechanism from killing essentially all developing oocytes. Supporting Evidence: PMID:11546739 It is also needed to prevent the physiological germline apoptosis mechanism killing essentially all developing oocytes, making lack of cgh-1 function the first stimulus identified that can trigger this mechanism

Gene Description

Proposed New Ontology Terms

maintenance of regulatory ncRNA-mediated transgenerational gene silencing

Existing Annotations Review

Core Functions

CGH-1 is a DEAD-box RNA helicase with conserved ATP-binding and helicase domains. Crystal structures (PDB:7DTJ, 7DTK) confirm the helicase fold. RNA helicase activity is inferred from sequence similarity to characterized orthologs (ISS).

CGH-1 functions in translational repression as a P-body component, inhibiting translation of target mRNAs. This is a conserved function of DDX6 family helicases.

CGH-1 protects developing oocytes from physiological germline apoptosis. Loss of cgh-1 was the first identified stimulus that triggers excessive germline apoptosis. This is a unique and defining function of CGH-1 in C. elegans germline development.

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