DHX30 is an ATP-dependent RNA helicase with cytosolic and mitochondrial populations. It binds RNA and supports mitochondrial large ribosomal subunit assembly in association with mitochondrial RNA granules and nucleoids. Its endogenous RNA substrates and the remodeling step used during assembly remain unresolved. Pathogenic variants can impair RNA-dependent ATP hydrolysis or RNA unwinding, alter stress-granule behavior and disrupt neurodevelopment.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0002151 G-quadruplex RNA binding | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the phylogenetically inherited G-quadruplex RNA-binding assertion. Reason: The literal IBD is at Eumetazoa node PTN001053965, ancestral to the human DHX30 lineage before the DHX30/DHX36 duplication. Experimental descendant G-quadruplex RNA-binding annotations support that placement; the family label alone is not a reason to reject it. No target-specific loss has been established. This inherited specificity is retained as non-core because the directly tested human RNA-remodeling and mitochondrial assembly mechanism has not established a physiological G-quadruplex substrate. The more specific G-quadruplex DNA-binding IBD (GO:0051880) is instead placed at sibling node PTN000433435 outside the DHX30 path; its narrower placement does not negate the broader inherited assertion. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN001053965 SUPPORTS TRANSFER The literal IBD is present at this ancestral node on the reconstructed human lineage. Experimental descendant records ground the ancestral assertion; the donor count and target self-inclusion are not failure criteria. Supporting Evidence: GO_REF:0000033 |
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | MODIFY | Summary: Specify RNA binding within the genuine nucleic-acid-binding domain assignment. Reason: IPR011545 is present in the official human protein and its current InterPro2GO mapping is broad nucleic-acid binding. Human DHX30 RNA association is directly demonstrated, providing a supported descendant term without inferring a specific RNA sequence or structure from the domain alone. Proposed replacements: RNA binding |
| GO:0003678 DNA helicase activity | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain inherited DNA-helicase activity without making it the physiological core. Reason: The DNA-helicase IBD at PTN001053965 is on the human lineage; its placement predates the DHX30/DHX36 duplication and is experimentally grounded in descendants. Independently, the mouse DHX30 source reports a purified-protein DNA untwisting experiment in its verified abstract, although its full assay was not recovered. These positive observations argue against dismissing the inference as a paralog error. Human DNA substrates and an in vivo DNA-remodeling role remain unestablished in the inspected evidence. The more specific G-quadruplex DNA-binding IBD (GO:0051880) is instead placed at sibling node PTN000433435 outside the DHX30 path; its narrower placement does not negate the broader inherited assertion. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN001053965 SUPPORTS TRANSFER The literal IBD is present at this ancestral node on the reconstructed human lineage. Experimental descendant records ground the ancestral assertion; the donor count and target self-inclusion are not failure criteria. |
| GO:0003682 chromatin binding | IDA PMID:18063578 The layered structure of human mitochondrial DNA nucleoids. | MARK AS OVER ANNOTATED | Summary: Preserve mitochondrial nucleoid association without calling it nuclear chromatin binding. Reason: The source directly identifies DHX30 in native and formaldehyde-crosslinked mitochondrial nucleoids and corroborates its gradient distribution. GO:0003682 specifically describes binding to the chromatin of the eukaryotic nucleus. The mitochondrial preparation does not establish that claim or direct DNA contact. Retain the positive nucleoid evidence under the existing mitochondrial-nucleoid annotation; this assessment does not deny a separately observed nuclear histone association. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | ACCEPT | Summary: Retain RNA binding from human RNA-interactome capture. Reason: The source describes covalent UV crosslinking and mRNA-interactome capture in proliferating human HeLa cells. The target assignment is retained with curator deference: the full target-level supplementary table was not independently recovered, but RNA association is clearly established for human DHX30 by independent targeted experiments. No poly(A)-tail specificity or regulatory outcome is inferred from capture. |
| GO:0003723 RNA binding | HDA PMID:22681889 The mRNA-bound proteome and its global occupancy profile on ... | ACCEPT | Summary: Retain RNA binding from human mRNA-proteome capture. Reason: The source used photoreactive-nucleotide-enhanced UV crosslinking and oligo(dT) purification in a human embryonic kidney cell line. Retain the curator-identified target interaction with independent human RNA-association corroboration; the complete target-level table was not independently read. Poly(A)+ transcript selection does not establish contact with the poly(A) tail or a particular transcript. |
| GO:0003723 RNA binding | IDA PMID:29100085 De Novo Missense Mutations in DHX30 Impair Global Translatio... | ACCEPT | Summary: Retain experimentally demonstrated RNA association. Reason: The 2017 study affinity-purified tagged human DHX30 ribonucleoproteins from HEK293T cells and measured AES, B4GAT1 and MRPL11 transcripts by RT-PCR. The RNA-recognition-motif variant reduced their recovery relative to wild type, with a GFP-mCherry control. This establishes RNA association but not purified affinity for a unique physiological substrate or 16S-rRNA specificity. Supporting Evidence: |
| GO:0003724 RNA helicase activity | IBA GO_REF:0000033 | ACCEPT | Summary: The inherited RNA-helicase activity agrees with direct human biochemistry. Reason: Human DHX30 descends from the literal RNA-helicase IBD at PTN001053965, and its sequence exactly matches the family alignment. Experimental descendant records include DHX30 itself, a legitimate source for the ancestral reconstruction. Later purified human DHX30 directly unwinds RNA in an ATP-dependent assay; the target self-source is not circularity. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN001053965 SUPPORTS TRANSFER The literal IBD is present at this ancestral node on the reconstructed human lineage. Experimental descendant records ground the ancestral assertion; the donor count and target self-inclusion are not failure criteria. |
| GO:0003724 RNA helicase activity | IDA PMID:29100085 De Novo Missense Mutations in DHX30 Impair Global Translatio... | ACCEPT | Summary: Retain RNA helicase activity with later direct biochemical corroboration. Reason: The imported 2017 paper assayed RNA-dependent ATP hydrolysis and RNA association; it did not itself report a duplex-unwinding experiment. The 2021 study directly showed ATP-dependent unwinding of a synthetic radiolabeled RNA duplex by purified full-length human His6-SUMO-DHX30 expressed in bacteria. Preserve the original GOA identity while explicitly distinguishing its evidence from the later direct assay. |
| GO:0003724 RNA helicase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Retain electronically assigned RNA-helicase activity. Reason: The current ARBA00028402 branch is satisfied by all three literal FunFam conditions on the human protein. EC:3.6.4.13 maps to RNA helicase activity, and the mouse ortholog is a legitimate separate transfer source. Direct human ATP-dependent RNA unwinding independently supports the molecular claim; rule matching alone is not treated as an experiment. |
| GO:0003725 double-stranded RNA binding | IDA PMID:21266579 Raftlin is involved in the nucleocapture complex to induce p... | KEEP AS NON CORE | Summary: Retain independently corroborated double-stranded RNA binding, with the original screen-specific gap explicit. Reason: The PMID:21266579 Methods describe sequential poly(U)/poly(I:C) capture from human Raji lysates, but its DHX30-specific supplementary hit remains unverified. Independent evidence supports the binding class: the official target sequence contains the DRBM region matched by IPR056755/PF24995, and purified full-length human DHX30 directly unwinds a radiolabeled RNA duplex in PMID:34020708. PDB 2DB2 is an NMR structure of the native 42–148 protein segment with terminal tags; it supports the domain fold, not an RNA-bound complex or a measured affinity. These convergent observations justify retaining the curator assertion as non-core without claiming recovery of the original target table, assigning the tested contact to a particular domain, or identifying a physiological dsRNA substrate. |
| GO:0005515 protein binding | IPI PMID:17932509 Proteomic and functional analysis of Argonaute-containing mR... | KEEP AS NON CORE | Summary: Retain RNA-dependent association with AGO2-containing mRNPs. Reason: The original Table 1 identifies DHX30 in AGO2 complexes II and III, and reciprocal tagged DDX30 co-immunoprecipitation is RNase-A-sensitive. This is positive mRNP association, not an independently demonstrated protein-only interface with the AGO2 nuclease. Retain the generic source assertion under the scoped project policy without assigning DHX30 nuclease, silencing or adaptor activity. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:17932509 Proteomic and functional analysis of Argonaute-containing mR... | KEEP AS NON CORE | Summary: Retain RNA-dependent association with AGO1-containing mRNPs. Reason: The original Table 1 and reciprocal co-immunoprecipitation identify DHX30 with AGO1; RNase A disrupts the association. The official AGO1 function record explicitly lacks endonuclease activity, so an enzyme-binding refinement is not supported by treating AGO1 like AGO2. Retain the positive mRNP association under the scoped project policy without inventing a direct interface or RNA-silencing role for DHX30. Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21903422 Mapping a dynamic innate immunity protein interaction networ... | MODIFY | Summary: Classify the observed PKR association by its established serine/threonine kinase partner. Reason: Two source-specific records include the network co-purification and a positive FLAG-DHX30/HA-PKR co-immunoprecipitation in human HEK293 cells. The original describes replicated affinity purification and orthogonal validation, while the official partner FUNCTION establishes PKR as a serine/threonine kinase. The refinement denotes the observed partner class, not DHX30-mediated kinase activation, phosphorylation or a purified binary interface. Proposed replacements: protein serine/threonine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21903422 Mapping a dynamic innate immunity protein interaction networ... | MODIFY | Summary: Classify the DHX58/LGP2 association as ATPase binding. Reason: The literal source records include positive tagged DHX30-DHX58 co-immunoprecipitation in HEK293 cells. The curated DHX58 catalytic record establishes ATP hydrolysis, satisfying the current ATPase-binding partner definition. This refinement does not assign helicase or antiviral signaling activity to DHX30, and does not imply that DHX58 possesses the CARD-dependent signaling initiation function it lacks. Proposed replacements: ATPase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:21903422 Mapping a dynamic innate immunity protein interaction networ... | MODIFY | Summary: Classify the positive OAS3 association as enzyme binding. Reason: The original-network records and source-specific tagged co-immunoprecipitation join DHX30 to OAS3 in HEK293 cells. Curated OAS3 function directly describes ATP oligoadenylate synthesis. Enzyme binding therefore describes a real catalytic partner class; it does not transfer OAS3 catalysis or RNase-L regulation to DHX30. Direct purified binding and native functional consequences were not established by these assays. Proposed replacements: enzyme binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:23455922 Interlaboratory reproducibility of large-scale human protein... | MODIFY | Summary: Refine the PKR complex association to serine/threonine kinase binding. Reason: The exact source-specific IntAct record identifies DHX30 with tandem-tagged human PKR in a HEK293 tandem-affinity purification. The verified abstract describes the standardized multi-laboratory kinase AP-MS study; full target-level original controls were not independently recovered. Retain positive curator-supported association and the independently established partner class, without claiming direct binary binding or kinase regulation. Proposed replacements: protein serine/threonine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | MODIFY | Summary: Refine the H1-5 association to histone binding. Reason: The literal source record identifies a DHX30-H1-5 crosslink in human U2OS nuclei. The original Methods use isolated nuclei and DSSO crosslinking, with analysis across nuclear preparations; the authors also discuss possible intercompartment contamination and post-lysis artifacts. H1-5 is an established linker histone. Retain this physical partner-class evidence without asserting that DHX30 is a chromatin structural component or has a particular nuclear regulatory function. Proposed replacements: histone binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:32707033 Kinase Interaction Network Expands Functional and Disease Ro... | MODIFY | Summary: Refine the independently captured PKR association to serine/threonine kinase binding. Reason: The source-specific positive record links DHX30 to N-terminal Strep-HA PKR in HEK293 Flp-In T-REx cells. The original AP-MS study used inducible bait expression, GFP controls and stringent statistical filtering. This supports association with an established serine/threonine kinase, without establishing direct contact, kinase activation or DHX30 phosphorylation. Proposed replacements: protein serine/threonine kinase binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | MODIFY | Summary: Refine the BioPlex H1-5 association to histone binding. Reason: The literal HEK293T record links DHX30 to C-terminally tagged H1-5 in the BioPlex affinity-purification network. Actual original Methods describe FLAG-HA capture and gene-level aggregation. H1-5 is a linker histone; the refined class is supported without claiming native chromatin remodeling, a purified interface or a particular natural DHX30 isoform. Proposed replacements: histone binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy... | MODIFY | Summary: Classify the mammalian two-hybrid CFTR interaction as transmembrane transporter binding. Reason: The exact source pair is human DHX30-CFTR in the mammalian split-ubiquitin assay. The original describes tagged ORFs, HEK293 reporter cells, frequent-flier control baits and replicate screening. CFTR is an experimentally established anion channel, satisfying the transmembrane-transporter binding definition. This does not establish channel regulation by DHX30, native colocalization of every isoform or an untagged biochemical affinity. Proposed replacements: transmembrane transporter binding Supporting Evidence: |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | KEEP AS NON CORE | Summary: Retain the CFTR-associated observation with the proximity-labeling limitation explicit. Reason: All four source-specific records are BioID proximity observations for tagged CFTR constructs, including G551D and a 1-1281 construct. The original explicitly labels both interacting and nearby proteins over a roughly 10-20 nm radius. It does not itself prove a binary DHX30-CFTR interaction. Independent mammalian split-ubiquitin evidence supports the same gene pair, so retain a conservative non-core association while keeping that corroboration separate from this proximity assay. No CFTR-regulatory function is inferred. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: Retain ATP binding as the helicase nucleotide interaction. Reason: The ATP-binding helicase domain is present and the current IPR011545 mapping includes ATP binding. Human DHX30 ATP hydrolysis and ATP-dependent RNA unwinding independently support the nucleotide interaction. ATP binding is part of this mechanism rather than a separate physiological core; it is not replaced across ontology branches by a catalytic activity. |
| GO:0005634 nucleus | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain ancestral nuclear localization as a non-core pool. Reason: The literal nucleus IBD at Eukaryota node PTN000717298 is on the reconstructed human lineage and has experimental descendant grounding. A human nuclear-preparation H1-5 crosslink independently corroborates a nuclear-associated population, with the original crosslinking and compartment-contamination limits preserved. Neither this ancestry nor that experiment resolves nucleoplasm versus chromatin occupancy, so no unsupported finer compartment is substituted. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000717298 SUPPORTS TRANSFER The literal IBD is present at this ancestral node on the reconstructed human lineage. Experimental descendant records ground the ancestral assertion; the donor count and target self-inclusion are not failure criteria. |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | MODIFY | Summary: Specify the independently established cytosolic pool. Reason: The literal cytoplasmic IBD at PTN002707150 is on the human lineage and is experimentally grounded, including target evidence. Human HPA data specifically support cytosol in A-431 and U-251MG cells. Use that supported descendant for the non-organelle pool without excluding the separately documented mitochondrial population. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002707150 SUPPORTS TRANSFER The literal IBD is present at this ancestral node on the reconstructed human lineage. Experimental descendant records ground the ancestral assertion; the donor count and target self-inclusion are not failure criteria. Proposed replacements: cytosol Supporting Evidence: GO_REF:0000033 GO_REF:0000052 |
| GO:0005737 cytoplasm | IDA PMID:29100085 De Novo Missense Mutations in DHX30 Impair Global Translatio... | MODIFY | Summary: Distinguish the diffuse cytosolic pool from endogenous stress-induced granule localization. Reason: Wild-type and endogenous DHX30 show a diffuse cytoplasmic pool in human U2OS cells, with a mitochondrial population also present. Independent HPA data identify cytosol in A-431 and U-251MG cells. In the same PMID:29100085 source, heat stress recruits endogenous DHX30 into granules; original Figure S5B shows partial colocalization with ATXN2 and DDX3X, supporting cytoplasmic stress granule. The cytosol and stress-granule replacements preserve the distinct diffuse and stress-induced pools without asserting exclusive localization, a FMRP-specific granule identity, or a demonstrated molecular assembly step. The HPA data record was inspected; the original S5B images were independently inspected. Proposed replacements: cytosol cytoplasmic stress granule Supporting Evidence: PMID:29100085 endogenous DHX30 also alters its diffuse cytoplasmic localization to accumulate in SGs GO_REF:0000052 |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | MODIFY | Summary: Refine broad electronic cytoplasm localization to the observed cytosolic pool. Reason: Current ARBA00026971 matching FunFam conditions, the SL-0086 mapping and mouse-ortholog context support broad cytoplasmic localization. The human HPA data identify a cytosolic population, allowing a supported specific replacement. This does not reclassify all mitochondrial signal as cytosol or establish isoform equivalence. Proposed replacements: cytosol Supporting Evidence: GO_REF:0000120 GO_REF:0000052 |
| GO:0005739 mitochondrion | EXP PMID:16825194 Human mitochondrial DNA nucleoids are linked to protein fold... | ACCEPT | Summary: Retain the experimentally grounded mitochondrial location. Reason: The verified original abstract reports HeLa nucleoid purification, DHX30 peptides, and antibody confirmation of mitochondrial localization of a specific product. Full original text was not recovered; do not infer exact construct endpoints or map its historical product name to a current UniProt isoform. Independent human microscopy and mitochondrial RNA-granule work corroborate the organelle-level claim. Supporting Evidence: PMID:16825194 confirmed the mitochondrial localization |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: Retain mitochondrial localization with the proteomic product groups distinguished. Reason: The original MitoCoP Table S1 includes DHX30 in the mitochondrial proteome. The Q7L2E3-2 protein group is class 1/cluster 1 and peripherally membrane-associated; a mixed canonical/isoform-3 group has class 5/cluster 2c and no assigned topology category. These data establish a mitochondrial population without resolving every product into matrix or nucleoid. The compiled matrix database column is not a new matrix-localization experiment. Supporting Evidence: |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | ACCEPT | Summary: Retain directly curated human mitochondrial staining. Reason: The inspected HPA data record identifies mitochondria as the main supported location, with U-251MG and U2OS annotations; A-431 and U-251MG also support cytosol. This source resolves the organelle but not a submitochondrial compartment. The record was read; image pixels were not independently scored. Supporting Evidence: GO_REF:0000052 |
| GO:0005739 mitochondrion | IDA PMID:29100085 De Novo Missense Mutations in DHX30 Impair Global Translatio... | ACCEPT | Summary: Retain the directly observed mitochondrial population. Reason: The original human U2OS study reports mitochondrial signal alongside diffuse cytoplasmic DHX30. It tested N- and C-terminal GFP constructs, including the paper's transcript variant 3 with a putative targeting extension. Those names are not equated to current UniProt isoform numbers without sequence correspondence. The evidence supports a mitochondrial pool, not an independently demonstrated submitochondrial matrix assay. Supporting Evidence: |
| GO:0005739 mitochondrion | IEA GO_REF:0000044 | ACCEPT | Summary: Retain the experimentally corroborated mitochondrial organelle mapping. Reason: The literal SL-0173-to-GO mapping is correct, and independent human imaging, nucleoid studies and mitochondrial RNA-granule experiments support the organelle. These broader localization observations need not be narrowed universally to one submitochondrial site; nucleoid and matrix annotations retain their distinct source scopes. |
| GO:0005759 mitochondrial matrix | IDA PMID:23275553 Alternative translation initiation augments the human mitoch... | ACCEPT | Summary: Retain the curated matrix location with explicit assay-resolution limits. Reason: The original human HEK293T study detects DHX30 in mitochondrial nucleic-acid-associated gradient fractions and shows its reduction after mitochondrial nucleic-acid depletion. Its separate matrix-fraction Figure 2C assays PABPC5, not DHX30. Retain the curator-supported matrix assignment in the coherent mitochondrial RNA/nucleoid context, while not misrepresenting that panel as direct DHX30 submitochondrial fractionation or claiming freely soluble residence. Independent MitoCoP peripheral association is compatible with, but does not prove, a matrix-facing location. |
| GO:0005829 cytosol | IDA GO_REF:0000052 | ACCEPT | Summary: Retain the independently curated human cytosolic population. Reason: The HPA record reports supported cytosolic staining in A-431 and U-251MG cells alongside mitochondrial staining in other observations. This is compatible with the distinct diffuse cytoplasmic population in the targeted human study. The data do not distinguish all three natural products and do not imply exclusive cytosolic localization. |
| GO:0007417 central nervous system development | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the developmental consequence of orthologous DHX30 function. Reason: The Ensembl Compara names mouse DHX30 Q99PU8 as the source. Its verified primary abstract describes neural expression and loss of brain and somite differentiation in homozygous embryos, with early lethality. Human neurodevelopmental disease independently supports conservation of developmental importance. Keep this downstream developmental process as non-core relative to RNA remodeling; neither expression alone nor the disease label identifies the exact CNS-specific biochemical step. The complete mouse original was not recovered. |
| GO:0007417 central nervous system development | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the developmental consequence of orthologous DHX30 function. Reason: The manual orthology transfer names mouse DHX30 Q99PU8 as the source. Its verified primary abstract describes neural expression and loss of brain and somite differentiation in homozygous embryos, with early lethality. Human neurodevelopmental disease independently supports conservation of developmental importance. Keep this downstream developmental process as non-core relative to RNA remodeling; neither expression alone nor the disease label identifies the exact CNS-specific biochemical step. The complete mouse original was not recovered. |
| GO:0016887 ATP hydrolysis activity | EXP PMID:29100085 De Novo Missense Mutations in DHX30 Impair Global Translatio... | ACCEPT | Summary: Retain RNA-stimulated ATP hydrolysis as part of the helicase mechanism. Reason: Tagged human DHX30 was immunopurified from HEK293T cells and assayed for released phosphate with and without exogenous yeast RNA, normalized to recovered protein. Several ATP-site variants reduced activity; the RNA-recognition variant Arg493His did not. ATP hydrolysis is experimentally established but is not itself proof of strand unwinding or a separate physiological core. Supporting Evidence: PMID:29100085 DHX30 hydrolyses ATP in an RNA-dependent fashion |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000120 | ACCEPT | Summary: Retain ATP hydrolysis despite a current rule-reconstruction limit. Reason: The literal RHEA:13065 mapping is ATP hydrolysis, matching direct human DHX30 biochemical measurements. The current ARBA00043426 response has no fully matching condition set in the inspected official target cross-references; this prevents claiming reproduction of that particular rule route, not rejection of the well-established activity or the independent Rhea mapping. |
| GO:0035770 ribonucleoprotein granule | IDA PMID:25683715 Mitochondrial RNA Granules Are Centers for Posttranscription... | ACCEPT | Summary: Retain mitochondrial RNA-granule localization. Reason: The original study used endogenous human DHX30 immunofluorescence with GRSF1 and newly synthesized RNA labeling. These observations support mitochondrial RNA-granule localization; they do not identify a unique bound RNA or a fixed granule stoichiometry. Supporting Evidence: |
| GO:0042645 mitochondrial nucleoid | IDA PMID:18063578 The layered structure of human mitochondrial DNA nucleoids. | ACCEPT | Summary: Retain direct mitochondrial nucleoid association. Reason: The actual original Table 1 places DHX30/NP_055781 among core nucleoid proteins, with peptide counts 6/16 in native preparations and 12/5 in the two crosslinked preparations. Target immunoblots further track nucleoids. This supports nucleoid localization without establishing a direct DNA contact, a DNA-remodeling mechanism or exclusive residence; formaldehyde can crosslink protein-protein associations. Supporting Evidence: |
| GO:0042645 mitochondrial nucleoid | IDA PMID:25683715 Mitochondrial RNA Granules Are Centers for Posttranscription... | ACCEPT | Summary: Retain the observed nucleoid-associated population with spatial limits. Reason: The original human imaging reports partial overlap with mitochondrial DNA puncta alongside stronger RNA-granule association. Preserve the curator's localization claim without converting spatial association into direct DNA binding, exclusive nucleoid residence or a DNA-unwinding mechanism. Supporting Evidence: |
| GO:0042645 mitochondrial nucleoid | IEA GO_REF:0000044 | ACCEPT | Summary: Retain the literal mitochondrial-nucleoid location mapping. Reason: SL-0269 maps to GO:0042645 and is supported by target-specific native/crosslinked nucleoid experiments and partial human mitochondrial-DNA colocalization. The evidence denotes a nucleoid-associated population, not obligatory DNA binding or stable membership in the mitoribosome. |
| GO:1902775 mitochondrial large ribosomal subunit assembly | IMP PMID:25683715 Mitochondrial RNA Granules Are Centers for Posttranscription... | ACCEPT | Summary: Retain participation in mitochondrial large-subunit assembly. Reason: Human DHX30 depletion impairs mitochondrial large-subunit and monosome assembly, with unassembled ribosomal proteins in lighter gradient fractions. RNA-granule localization supports an assembly-factor role. The study did not establish DHX30 as a stable structural ribosomal subunit or identify its particular RNA-remodeling substrate. Supporting Evidence: |
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Download this section (compressed HTML)Q: Which endogenous RNAs are remodeled by DHX30 during mitochondrial large-subunit assembly, and which remodeling step directly requires its ATP-dependent helicase activity?
Q: How do the three current natural sequence products partition between cytosol, mitochondria and nucleoid-associated RNA granules, and which historical transcript constructs correspond exactly to them?
Q: Do human DHX30 DNA-helicase and G-quadruplex-binding activities have physiological substrates distinct from its RNA-remodeling role?
Q: What target-level evidence in the supplementary poly(I:C)-capture list supports the DHX30 dsRNA-binding assignment?
Q: Which RNA-remodeling, structural or cofactor step does wild-type DHX30 perform during stress-granule formation, as distinct from its recruitment or indirect effects on translation and stress signaling?
Experiment: Map endogenous product-specific RNA contacts together with mitochondrial large-subunit assembly intermediates, using selective depletion and rescue with sequence-verified wild-type and catalytic-defective products.
Experiment: Compare purified sequence-verified human products on matched RNA, DNA and G-quadruplex substrates, then test the identified contacts in intact cells without assuming that in-vitro substrate activity defines a physiological process.
Experiment: Rescue DHX30-depleted cells with matched, sequence-verified wild-type and catalytic or RNA-binding mutants while measuring translation, stress signaling and granule nucleation separately. Combine these measurements with defined RNA/protein assembly assays to identify any DHX30-performed step rather than infer it from granule counts alone.
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