ArticlePlant physiology2012
The helicase and RNaseIIIa domains of Arabidopsis Dicer-Like1 modulate catalytic parameters during microRNA biogenesis.
Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed, 92 citations in OpenAlex.
- Transposon expansion is associated with reorganization of small RNA and DNA methylation landscapes in the morphologically minimal angiosperm Wolffia brasiliensis.The Plant journal : for cell and molecular biology · 2026Article
- Plant microRNA maturation and function.Nature reviews. Molecular cell biology · 2026Review
- Key RNA elements influencing DCL1 cleavage in plant microRNA biogenesis.Nature plants · 2025Article
- Identification and characterization of DICER-LIKE genes and their roles in Marchantia polymorpha development and salt stress response.The Plant journal : for cell and molecular biology · 2025Article
- MicroRNAs in Plant Genetic Regulation of Drought Tolerance and Their Function in Enhancing Stress Adaptation.Plants (Basel, Switzerland) · 2025Review
- Artificial miRNAs and target-mimics as potential tools for crop improvement.Physiology and molecular biology of plants : an international journal of functional plant biology · 2025Review
- The human Dicer helicase domain is capable of ATP hydrolysis and single-stranded nucleic acid binding.BMC biology · 2024Article
- Genome-wide identification, characterization and expression analysis of key gene families in RNA silencing in centipedegrass.BMC genomics · 2024Article
- Evidence for an RNAi-independent role of Arabidopsis DICER-LIKE2 in growth inhibition and basal antiviral resistance.The Plant cell · 2024Article
- Article
- The HIGH EXPRESSION OF OSMOTICALLY RESPONSIVE GENE15-HISTONE DEACETYLASE9 complex associates with HYPONASTIC LEAVES 1 to modulate microRNA expression in response to abscisic acid signaling.The Plant cell · 2023Article
- Dicer structure and function: conserved and evolving features.EMBO reports · 2023Review
- MicroRNA156 conditions auxin sensitivity to enable growth plasticity in response to environmental changes in Arabidopsis.Nature communications · 2023Article
- microRNA production inFrontiers in plant science · 2023Review
- Uridylation and the SKI complex orchestrate the Calvin cycle of photosynthesis through RNA surveillance ofProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Transcriptional and post-transcriptional regulation of RNAi-related gene expression during plant-virus interactions.Stress biology · 2022Review
- Arabidopsis RBV is a conserved WD40 repeat protein that promotes microRNA biogenesis and ARGONAUTE1 loading.Nature communications · 2022Article
- MicroRNA biogenesis and activity in plant cell dedifferentiation stimulated by cell wall removal.BMC plant biology · 2022Article
- Mechanisms of MicroRNA Biogenesis and Stability Control in Plants.Frontiers in plant science · 2022Review
- Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dicer-Like1 (DCL1), an RNaseIII endonuclease, and Hyponastic Leaves1 (HYL1), a double-stranded RNA-binding protein, are core components of the plant microRNA (miRNA) biogenesis machinery. hyl1 null mutants accumulate low levels of miRNAs and display pleiotropic developmental phenotypes. We report the identification of five new hyl1 suppressor mutants, all of which are alleles of DCL1. These new alleles affect either the helicase or the RNaseIIIa domains of DCL1, highlighting the critical functions of these domains. Biochemical analysis of the DCL1 suppressor variants reveals that they process the primary transcript (pri-miRNA) more efficiently than wild-type DCL1, with both higher K(cat) and lower K(m) values. The DCL1 variants largely rescue wild-type miRNA accumulation levels in vivo, but do not rescue the MIRNA processing precision defects of the hyl1 null mutant. In vitro, the helicase domain confers ATP dependence on DCL1-catalyzed MIRNA processing, attenuates DCL1 cleavage activity, and is required for precise MIRNA processing of some substrates.
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Registered trials
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.