ArticlePloS one2015
A unique HMG-box domain of mouse Maelstrom binds structured RNA but not double stranded DNA.
Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Molecular insights into the Drosophila piRNA pathway via systematic ReLo protein interaction screening and structure prediction.Nucleic acids research · 2025Article
- Long non-coding RNAs: definitions, functions, challenges and recommendations.Nature reviews. Molecular cell biology · 2023Review
- Retrotransposon LINE-1 bodies in the cytoplasm of piRNA-deficient mouse spermatocytes: Ribonucleoproteins overcoming the integrated stress response.PLoS genetics · 2023Article
- The DNA-Binding High-Mobility Group Box Domain of Sox Family Proteins Directly Interacts with RNABiochemistry · 2022Article
- Maelstrom functions in the production of Siwi-piRISC capable of regulating transposons iniScience · 2022Article
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- Alternate Roles of Sox Transcription Factors beyond Transcription Initiation.International journal of molecular sciences · 2021Review
- Multi-omic analysis elucidates the genetic basis of hydrocephalus.Cell reports · 2021Article
- Mael is essential for cancer cell survival and tumorigenesis through protection of genetic integrity.Oncotarget · 2017Article
- Multiple LINEs of retrotransposon silencing mechanisms in the mammalian germline.Seminars in cell & developmental biology · 2016Review
- The DNA binding high mobility group box protein family functionally binds RNA.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Piwi-interacting piRNAs are a major and essential class of small RNAs in the animal germ cells with a prominent role in transposon control. Efficient piRNA biogenesis and function require a cohort of proteins conserved throughout the animal kingdom. Here we studied Maelstrom (MAEL), which is essential for piRNA biogenesis and germ cell differentiation in flies and mice. MAEL contains a high mobility group (HMG)-box domain and a Maelstrom-specific domain with a presumptive RNase H-fold. We employed a combination of sequence analyses, structural and biochemical approaches to evaluate and compare nucleic acid binding of mouse MAEL HMG-box to that of canonical HMG-box domain proteins (SRY and HMGB1a). MAEL HMG-box failed to bind double-stranded (ds)DNA but bound to structured RNA. We also identified important roles of a novel cluster of arginine residues in MAEL HMG-box in these interactions. Cumulatively, our results suggest that the MAEL HMG-box domain may contribute to MAEL function in selective processing of retrotransposon RNA into piRNAs. In this regard, a cellular role of MAEL HMG-box domain is reminiscent of that of HMGB1 as a sentinel of immunogenic nucleic acids in the innate immune response.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.