AgrobacTransV1, Main, Exploration, bibRecord, 000741

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

Identifieur interne : 000741 ( Main/Exploration ); précédent : 000740; suivant : 000742

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

Auteurs : Yukio Kurihara [Japon] ; Yuasa Takashi ; Yuichiro Watanabe

Source :

RNA (New York, N.Y.) [ 1355-8382 ] ; 2006.

RBID : pubmed:16428603

Descripteurs français

English descriptors

KwdEn :
- Arabidopsis (genetics), Arabidopsis Proteins (genetics), Arabidopsis Proteins (metabolism), Base Sequence (MeSH), Binding Sites (MeSH), Cell Cycle Proteins (genetics), Cell Cycle Proteins (metabolism), Gene Expression Regulation, Plant (MeSH), MicroRNAs (genetics), MicroRNAs (metabolism), Molecular Sequence Data (MeSH), Mutation (MeSH), RNA Processing, Post-Transcriptional (MeSH), RNA, Double-Stranded (metabolism), RNA-Binding Proteins (genetics), RNA-Binding Proteins (metabolism), Rhizobium (genetics), Ribonuclease III (genetics), Ribonuclease III (metabolism), Tobacco (genetics).
MESH :
- chemical , genetics : Arabidopsis Proteins, Cell Cycle Proteins, MicroRNAs, RNA-Binding Proteins, Ribonuclease III.
- genetics : Arabidopsis, Rhizobium, Tobacco.
- chemical , metabolism : Arabidopsis Proteins, Cell Cycle Proteins, MicroRNAs, RNA, Double-Stranded, RNA-Binding Proteins, Ribonuclease III.
- Base Sequence, Binding Sites, Gene Expression Regulation, Plant, Molecular Sequence Data, Mutation, RNA Processing, Post-Transcriptional.

Abstract

It has been reported that some double-stranded RNA (dsRNA) binding proteins interact with small RNA biogenesis-related RNase III enzymes. However, their biological significance is poorly understood. Here we examine the relationship between the Arabidopsis microRNA- (miRNA) producing enzyme DCL1 and the dsRNA binding protein HYL1. In the hyl1-2 mutant, the processing steps of miR163 biogenesis were partially impaired; increased accumulation of pri-miR163 and reduced accumulation of short pre-miR163 and mature miR163 as well as misplaced cleavages in the stem structure of pri-miR163 were detected. These misplaced cleavages were similar to those previously observed in the dcl1-9 mutant, in which the second double-stranded RNA binding domain of the protein was disrupted. An immunoprecipitation assay using Agrobacterium-mediated transient expression in Nicotiana benthamiana showed that HYL1 was able to form a complex with wild-type DCL1 protein, but not with the dcl1-9 mutant protein. We also examined miR164b and miR166a biogenesis in hyl1-2 and dcl1-9. Increased accumulation of pri-miRNAs and reduced accumulation of pre-miRNAs and mature miRNAs were detected. Misplaced cleavage on pri-miR164b was observed only in dcl1-9 but not in hyl1-2, whereas not on pri-miR166a in either mutant. These results indicate that HYL1 has a function in assisting efficient and precise cleavage of pri-miRNA through interaction with DCL1.

DOI: 10.1261/rna.2146906
PubMed: 16428603
PubMed Central: PMC1370900

Affiliations:

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Le document en format XML

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<front><div type="abstract" xml:lang="en">It has been reported that some double-stranded RNA (dsRNA) binding proteins interact with small RNA biogenesis-related RNase III enzymes. However, their biological significance is poorly understood. Here we examine the relationship between the Arabidopsis microRNA- (miRNA) producing enzyme DCL1 and the dsRNA binding protein HYL1. In the hyl1-2 mutant, the processing steps of miR163 biogenesis were partially impaired; increased accumulation of pri-miR163 and reduced accumulation of short pre-miR163 and mature miR163 as well as misplaced cleavages in the stem structure of pri-miR163 were detected. These misplaced cleavages were similar to those previously observed in the dcl1-9 mutant, in which the second double-stranded RNA binding domain of the protein was disrupted. An immunoprecipitation assay using Agrobacterium-mediated transient expression in Nicotiana benthamiana showed that HYL1 was able to form a complex with wild-type DCL1 protein, but not with the dcl1-9 mutant protein. We also examined miR164b and miR166a biogenesis in hyl1-2 and dcl1-9. Increased accumulation of pri-miRNAs and reduced accumulation of pre-miRNAs and mature miRNAs were detected. Misplaced cleavage on pri-miR164b was observed only in dcl1-9 but not in hyl1-2, whereas not on pri-miR166a in either mutant. These results indicate that HYL1 has a function in assisting efficient and precise cleavage of pri-miRNA through interaction with DCL1.</div>
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EXPLOR_STEP=$WICRI_ROOT/Bois/explor/AgrobacTransV1/Data/Main/Exploration

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000741 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000741 | SxmlIndent | more

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{{Explor lien
   |wiki=    Bois
   |area=    AgrobacTransV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:16428603
   |texte=   The interaction between DCL1 and HYL1 is important for efficient and precise processing of pri-miRNA in plant microRNA biogenesis.
}}

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HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:16428603" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a AgrobacTransV1

This area was generated with Dilib version V0.6.38.
Data generation: Fri Nov 20 15:45:55 2020. Site generation: Wed Mar 6 15:24:41 2024

	Serveur d'exploration sur l'agrobacterium et la transgénèse
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Serveur d'exploration sur l'agrobacterium et la transgénèse

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

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

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