DHX30 is an ATP-dependent RNA helicase with mitochondrial and cytosolic populations. The 2017 human study demonstrates RNA-dependent ATP hydrolysis and RNA association; the later 2021 study directly demonstrates RNA duplex unwinding with purified full-length protein. These are complementary experiments, not interchangeable descriptions of one assay. The 2017 editorial correction changes an author's surname only. PMID:29100085(https://pmc.ncbi.nlm.nih.gov/articles/PMC5673606/), PMID:34020708(https://pmc.ncbi.nlm.nih.gov/articles/PMC8140440/), PMID:29304375(https://pubmed.ncbi.nlm.nih.gov/29304375/)
Mitochondrial DHX30 associates with RNA granules and partly overlaps nucleoids. Depletion impairs large ribosomal subunit and monosome assembly. Its mitochondrial RNA immunoprecipitation is broadly distributed; the specific 16S-rRNA result belongs to other factors in that study. A direct endogenous remodeling substrate remains unresolved, and DHX30 is not established as a stable structural mitoribosomal subunit. RNA binding and ATP hydrolysis are components of the RNA-helicase mechanism, not separate physiological cores. PMID:25683715(https://doi.org/10.1016/j.celrep.2015.01.030)
The official products contain 1,194, 1,222 and 1,155 residues. Their distinct N termini were reconstructed from the official sequence features. Historical transcript-variant names and full-length assay constructs have not been mapped unambiguously to all three current products. Neither activity equivalence nor inactivity is inferred from length. MitoCoP distinguishes a mixed canonical/isoform-3 protein group from a mitochondrial-enriched isoform-2 group, which is operationally peripheral membrane-associated. This is not a measurement of membrane face or proof of freely soluble matrix residence. The separate curated matrix assertion is retained with its source limits: Figure 2C of the alternative-initiation paper tests PABPC5, whereas its Figure 3B includes DHX30 in nucleic-acid-associated mitochondrial fractions. UniProt Q7L2E3, PMID:34800366(https://pmc.ncbi.nlm.nih.gov/articles/PMC8664129/), PMID:23275553(https://pmc.ncbi.nlm.nih.gov/articles/PMC3575844/)
The nucleoid preparation in the 2008 study supports mitochondrial association and does not establish binding to the chromatin of the eukaryotic nucleus. Separately, nuclear crosslinking identifies an H1-5 association, with the preparation and post-lysis limits retained. The inherited nuclear location is kept without inventing a finer nuclear compartment. PMID:18063578(https://doi.org/10.1074/jbc.M708444200), PMID:30021884(https://pmc.ncbi.nlm.nih.gov/articles/PMC6166682/)
Ancestral DNA-helicase and G-quadruplex RNA-binding assertions are not rejected merely because the family includes DHX36. The target lies below the actual asserted nodes, and experimental descendant records ground them. A separate mouse DHX30 abstract reports purified-protein DNA untwisting and developmental phenotypes. Human physiological DNA and G-quadruplex substrates remain unresolved, so these are non-core activities. The current FlyBase query's lack of matching experimental rows does not establish absence of historical curator support. GO_REF:0000033, PMID:25219788(https://doi.org/10.1089/scd.2014.0077)
AGO1/AGO2 association is RNA-sensitive, and the CFTR proximity-labeling observations do not by themselves establish a binary interface. Supported PKR, DHX58, OAS3, H1-5 and mammalian two-hybrid CFTR pairs permit partner-class refinements without transferring catalytic or signaling activities to DHX30. The generic positive associations retained as non-core follow the user's scoped project instruction. The dsRNA capture assertion remains unresolved because the relevant target supplementary table could not be recovered; this is not a wrong-gene inference from the article title. PMID:17932509(https://pmc.ncbi.nlm.nih.gov/articles/PMC2247381/), PMID:21903422(https://pmc.ncbi.nlm.nih.gov/articles/PMC3253658/), PMID:35156780(https://pmc.ncbi.nlm.nih.gov/articles/PMC8842165/), PMID:36012204(https://pmc.ncbi.nlm.nih.gov/articles/PMC9408702/), PMID:21266579(https://pmc.ncbi.nlm.nih.gov/articles/PMC3060521/)
The ordinary Falcon research request and configured fallback were attempted and failed; no provider report was fabricated. Manual primary-source assessment, raw record reconstruction and the independent chemistry consultation supplied this review. Cached publication bytes and original GOA identities were preserved. Cache availability flags describe the cache, while separate original access is recorded explicitly. Public assay locators and raw table facts are in the evidence guide and selected primary-source notes.
The earlier unresolved dsRNA-screen assessment is now distinguished from the gene-level function. The target-specific PMID:21266579 supplementary hit remains unverified. Independently, DHX30 contains a DRBM-domain match (IPR056755/PF24995), its native 42–148 region forms the protein-only NMR construct in PDB 2DB2, and purified full-length human protein unwinds an RNA duplex. This supports non-core dsRNA binding without claiming that the NMR experiment contained RNA, measured an affinity or established the contact domain. PMID:21266579(https://pmc.ncbi.nlm.nih.gov/articles/PMC3060521/), PMID:34020708(https://pmc.ncbi.nlm.nih.gov/articles/PMC8140440/), InterPro IPR056755
Wild-type stress-granule localization is distinct from pathological mutant aggregation. The original 2017 supplement, page 15 Figure S5B, shows endogenous DHX30 partially entering ATXN2- and DDX3X-positive granules after stress, with an unstressed comparison. Its cytoplasm annotation is refined to both the diffuse cytosolic pool and the stress-induced granule pool, without exclusive localization or a FMRP-specific identity. The source-specific refinement supplies component coverage without adding a redundant NEW row. PMID:29100085(https://doi.org/10.1016/j.ajhg.2017.09.014), original Figure S5
The later human HEK293T depletion and zebrafish knockout experiments also show reduced granule formation. These positive results are retained, but granule counts, recruitment and mutant-driven foci do not identify a molecular step that wild-type DHX30 performs in assembling the granule. No NEW stress-granule assembly process or additional core is asserted until an RNA-remodeling, structural or cofactor role is distinguished from effects on translation or stress signaling. DDX3X and DDX6 provide positive annotation comparators, so this is a target-evidence limit rather than a general convention excluding helicases. The inspected GO-CAM index has no target match. PMID:34020708(https://pmc.ncbi.nlm.nih.gov/articles/PMC8140440/), GO:0034063
The inherited RNA-G4 and DNA-helicase assertions originate at PTN001053965 before the DHX30/DHX36 duplication. The narrower DNA-G4-binding assertion at PTN000433435 belongs to a sibling lineage and is not inherited by human DHX30; this distinction does not establish loss of the broader activities. The CFTR MaMTH pair remains a supported transporter-class association, while the separate BioID source retains its proximity-only interpretation. GO_REF:0000033, PMID:35156780(https://pmc.ncbi.nlm.nih.gov/articles/PMC8842165/), PMID:36012204(https://pmc.ncbi.nlm.nih.gov/articles/PMC9408702/)
The natural products differ in their N termini: canonical 1194 aa; a 1222-aa product replacing the first 41 residues with 69 residues; and a 1155-aa product lacking the first 39 residues with an SR-to-MA replacement at the next two positions. Historical transcript-variant labels and assay constructs are not independently equated to all current accessions, and these sequence differences do not establish functional equivalence or inactivity. UniProt Q7L2E3