ArticleBiology direct2008
Functional insight into Maelstrom in the germline piRNA pathway: a unique domain homologous to the DnaQ-H 3'-5' exonuclease, its lineage-specific expansion/loss and evolutionarily active site switch.
Article in Biology direct, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 67 citations in OpenAlex.
- Integrative genomics elucidates the evolutionary, temporal, and developmental origins of a hydrocephalus risk gene.medRxiv : the preprint server for health sciences · 2025Article
- The functions and mechanisms of piRNAs in mediating mammalian spermatogenesis and their applications in reproductive medicine.Cellular and molecular life sciences : CMLS · 2024Review
- Article
- Target-specific requirements for RNA interference can arise through restricted RNA amplification despite the lack of specialized pathways.bioRxiv : the preprint server for biology · 2024Article
- Testicular piRNA Analysis Identified Dysregulated piRNAs in Non-obstructive Azoospermia.Reproductive sciences (Thousand Oaks, Calif.) · 2024Article
- Article
- Morphine suppresses the immune function of lung cancer by up-regulating MAEL expression.BMC pharmacology & toxicology · 2022Article
- Maelstrom functions in the production of Siwi-piRISC capable of regulating transposons iniScience · 2022Article
- Article
- MAEL Cancer-Testis Antigen as a Diagnostic Marker in Primary Stages of Gastric Cancer with Helicobacter pylori Infection.Journal of gastrointestinal cancer · 2020Article
- Maelstrom Represses Canonical Polymerase II Transcription within Bi-directional piRNA Clusters in Drosophila melanogaster.Molecular cell · 2019Article
- Gene Expression Profiling Reveals Potential Players of Left-Right Asymmetry in Female Chicken Gonads.International journal of molecular sciences · 2017Article
- The small non-coding RNA processing machinery of two living fossil species, lungfish and coelacanth, gives new insights into the evolution of the Argonaute protein family.Genome biology and evolution · 2017Article
- Metazoan Maelstrom is an RNA-binding protein that has evolved from an ancient nuclease active in protists.RNA (New York, N.Y.) · 2015Article
- A unique HMG-box domain of mouse Maelstrom binds structured RNA but not double stranded DNA.PloS one · 2015Article
- Primary piRNA biogenesis: caught up in a Maelstrom.The EMBO journal · 2014Article
- Reduced pachytene piRNAs and translation underlie spermiogenic arrest in Maelstrom mutant mice.The EMBO journal · 2014Article
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- piRNA and spermatogenesis in mice.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Review
- Article
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Maelstrom (MAEL) plays a crucial role in a recently-discovered piRNA pathway; however its specific function remains unknown. Here a novel MAEL-specific domain characterized by a set of conserved residues (Glu-His-His-Cys-His-Cys, EHHCHC) was identified in a broad range of species including vertebrates, sea squirts, insects, nematodes, and protists. It exhibits ancient lineage-specific expansions in several species, however, appears to be lost in all examined teleost fish species. Functional involvement of MAEL domains in DNA- and RNA-related processes was further revealed by its association with HMG, SR-25-like and HDAC_interact domains. A distant similarity to the DnaQ-H 3'-5' exonuclease family with the RNase H fold was discovered based on the evidence that all MAEL domains adopt the canonical RNase H fold; and several protist MAEL domains contain the conserved 3'-5' exonuclease active site residues (Asp-Glu-Asp-His-Asp, DEDHD). This evolutionary link together with structural examinations leads to a hypothesis that MAEL domains may have a potential nuclease activity or RNA-binding ability that may be implicated in piRNA biogenesis. The observed transition of two sets of characteristic residues between the ancestral DnaQ-H and the descendent MAEL domains may suggest a new mode for protein function evolution called "active site switch", in which the protist MAEL homologues are the likely evolutionary intermediates due to harboring the specific characteristics of both 3'-5' exonuclease and MAEL domains.
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Registered trials
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