Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

The N-terminal double-stranded RNA binding domains of Arabidopsis HYPONASTIC LEAVES1 are sufficient for pre-microRNA processing.

The Plant cell - 1 Mar 2007

Wu Feijie, Yu Lin, Cao Wenguang, Mao Yanfei, Liu Zhongyuan, He Yuke

Abstract excerpt

Arabidopsis thaliana HYPONASTIC LEAVES1 (HYL1) is a microRNA (miRNA) biogenesis protein that contains two N-terminal double-stranded RNA binding domains (dsRBDs), a putative nuclear localization site (NLS), and a putative protein-protein interaction domain. The interaction of HYL1 with DICER-LIKE...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Cell Nucleus
Share to MicroRNAs
Share to RNA-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to RNA, Double-Stranded

Share to RNA Precursors

Share to RNA Processing, Post-Transcriptional

Share to Structure-Activity Relationship

Share to Subcellular Fractions

Source

Open in PubMed Open full text

Identifiers

PMID: 17337628
DOI: 10.1105/tpc.106.048637
PMCID: PMC1867364

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 2 Sept 2026. Prepared record publication-17337628-2026-09-02.2. Manifest publication-graph-cohort-2026-09-02.2.

Source receipt: PubMed via Helena Literature Corpus, retrieved 2 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The N-terminal double-stranded RNA binding domains of Arabidopsis HYPONASTIC LEAVES1 are sufficient for pre-microRNA processing.PMID 17337628Read ↗

Structural determinants of Arabidopsis thaliana Hyponastic leaves 1 function in vivo.Semantic proximity Read ↗

A dominant mutation in DCL1 suppresses the hyl1 mutant phenotype by promoting the processing of miRNA.Semantic proximity Read ↗

The nuclear dsRNA binding protein HYL1 is required for microRNA accumulation and plant development, but not posttranscriptional transgene silencing.Semantic proximity Read ↗

Transcriptome analyses revealed diverse expression changes in ago1 and hyl1 Arabidopsis mutants.Semantic proximity Read ↗

The Arabidopsis double-stranded RNA-binding protein HYL1 plays a role in microRNA-mediated gene regulation.Semantic proximity Read ↗

The helicase and RNaseIIIa domains of Arabidopsis Dicer-Like1 modulate catalytic parameters during microRNA biogenesis.Semantic proximity Read ↗

Gene structures and processing of Arabidopsis thaliana HYL1-dependent pri-miRNAs.Semantic proximity Read ↗

The interaction between DCL1 and HYL1 is important for efficient and precise processing of pri-miRNA in plant microRNA biogenesis.Semantic proximity Read ↗

Arabidopsis primary microRNA processing proteins HYL1 and DCL1 define a nuclear body distinct from the Cajal body.Semantic proximity Read ↗

Arabidopsis AAR2, a conserved splicing factor in eukaryotes, acts in microRNA biogenesisSemantic proximity Read ↗

Intron Lariat RNA Inhibits MicroRNA Biogenesis by Sequestering the Dicing Complex in Arabidopsis.Semantic proximity Read ↗

The action of ARGONAUTE1 in the miRNA pathway and its regulation by the miRNA pathway are crucial for plant development.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.