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We are analyzing https://link.springer.com/article/10.1007/s11103-006-9125-8.

Title:
The dsRNA-binding protein DRB4 interacts with the Dicer-like protein DCL4 in vivo and functions in the trans-acting siRNA pathway | Plant Molecular Biology
Description:
Arabidopsis thaliana encodes four Dicer-like (DCL) proteins and five dsRNA-binding (DRB) proteins. We have previously demonstrated that DCL4 specifically interacts with DRB4 in vitro. Here we describe the interaction between DCL4 and DRB4 in vivo. The phenotype of a mutant with a defect in DCL4 (dcl4-2) was similar to that of a mutant with a defect in DRB4 (drb4-1): both mutant plants had elongated and downwardly curled rosette leaves and over-accumulated anthocyanin. In immunoprecipitation experiments with either anti-DCL4 or anti-DRB4 antibody and crude extracts of wild-type Arabidopsis plants, co-immunoprecipitation of DCL4 and DRB4 was detected, indicating that DCL4 interacts with DRB4 in vivo. This interaction was confirmed by immunoprecipitation experiments using extracts from dcl4-2, drb4-1, or transgenic plants expressing the hemagglutinin-tagged version of DCL4 or DRB4. The results of immunoprecipitation experiments also suggest that most DCL4 is associated with DRB4, but that some DRB4 is free or associated with other proteins. Reduced accumulation of the TAS1 and TAS3 trans-acting siRNA (ta-siRNA) and over accumulation of their target mRNAs (At5g18040 and auxin response factors ARF3 and ARF4) were detected in both drb4-1 and dcl4-2 mutants. These results indicate that DRB4, together with DCL4, functions in the ta-siRNA biogenesis.
Website Age:
28 years and 1 months (reg. 1997-05-29).

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  • Education
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Custom-built

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🌠 Phenomenal Traffic: 5M - 10M visitors per month


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Keywords {🔍}

article, google, scholar, pubmed, cas, dcl, protein, drb, arabidopsis, plant, dicerlike, rna, biol, proteins, transacting, plants, dsrnabinding, biogenesis, processing, research, functions, thaliana, small, sirnas, microrna, privacy, cookies, content, interacts, sirna, pathway, hiraguri, fukuhara, interaction, access, doublestranded, gene, nature, science, function, information, publish, search, vivo, nakazawa, tasirna, rnabinding, hyl, micrornas, gasciolli,

Topics {✒️}

hyl1/drb-family dsrna-binding proteins double-stranded rna-cleaving enzymes tas3 trans-acting sirna month download article/chapter producing trans-acting sirnas trans-acting sirna pathway hiromitsu moriyama & toshiyuki fukuhara arabidopsis micro-rna biogenesis lna-modified oligonucleotide probes microrna-mediated gene regulation trans-acting sirnas ta-sirna biogenesis small antisense rna wild-type arabidopsis plants environmental response-specific expression post-transcriptional gene silencing protein network research full article pdf small rna pathways antiviral defense agrobacterium-mediated transformation plant microrna biogenesis dsrna-binding privacy choices/manage cookies endogenous sirnas derived generating viral sirnas small rna processing dicer-1-loquacious complex electronic supplementary material ta-sirna related subjects dcl4 specifically interacts applied biological sciences article nakazawa viral defence pathway european economic area check access gregory ri dna methylation patterning dexh-box helicase instant access incomplete drb4-dependence posttranscriptional transgene silencing conditions privacy policy protein drb normal microrna maturation transgenic plants expressing hemagglutinin-tagged version anti-drb4 antibody protein dcl4

Schema {🗺️}

WebPage:
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         headline:The dsRNA-binding protein DRB4 interacts with the Dicer-like protein DCL4 in vivo and functions in the trans-acting siRNA pathway
         description: Arabidopsis thaliana encodes four Dicer-like (DCL) proteins and five dsRNA-binding (DRB) proteins. We have previously demonstrated that DCL4 specifically interacts with DRB4 in vitro. Here we describe the interaction between DCL4 and DRB4 in vivo. The phenotype of a mutant with a defect in DCL4 (dcl4-2) was similar to that of a mutant with a defect in DRB4 (drb4-1): both mutant plants had elongated and downwardly curled rosette leaves and over-accumulated anthocyanin. In immunoprecipitation experiments with either anti-DCL4 or anti-DRB4 antibody and crude extracts of wild-type Arabidopsis plants, co-immunoprecipitation of DCL4 and DRB4 was detected, indicating that DCL4 interacts with DRB4 in vivo. This interaction was confirmed by immunoprecipitation experiments using extracts from dcl4-2, drb4-1, or transgenic plants expressing the hemagglutinin-tagged version of DCL4 or DRB4. The results of immunoprecipitation experiments also suggest that most DCL4 is associated with DRB4, but that some DRB4 is free or associated with other proteins. Reduced accumulation of the TAS1 and TAS3 trans-acting siRNA (ta-siRNA) and over accumulation of their target mRNAs (At5g18040 and auxin response factors ARF3 and ARF4) were detected in both drb4-1 and dcl4-2 mutants. These results indicate that DRB4, together with DCL4, functions in the ta-siRNA biogenesis.
         datePublished:2007-01-14T00:00:00Z
         dateModified:2007-01-14T00:00:00Z
         pageStart:777
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            DRB4
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            Protein–protein interaction
            ta-siRNA
            Plant Sciences
            Biochemistry
            general
            Plant Pathology
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      headline:The dsRNA-binding protein DRB4 interacts with the Dicer-like protein DCL4 in vivo and functions in the trans-acting siRNA pathway
      description: Arabidopsis thaliana encodes four Dicer-like (DCL) proteins and five dsRNA-binding (DRB) proteins. We have previously demonstrated that DCL4 specifically interacts with DRB4 in vitro. Here we describe the interaction between DCL4 and DRB4 in vivo. The phenotype of a mutant with a defect in DCL4 (dcl4-2) was similar to that of a mutant with a defect in DRB4 (drb4-1): both mutant plants had elongated and downwardly curled rosette leaves and over-accumulated anthocyanin. In immunoprecipitation experiments with either anti-DCL4 or anti-DRB4 antibody and crude extracts of wild-type Arabidopsis plants, co-immunoprecipitation of DCL4 and DRB4 was detected, indicating that DCL4 interacts with DRB4 in vivo. This interaction was confirmed by immunoprecipitation experiments using extracts from dcl4-2, drb4-1, or transgenic plants expressing the hemagglutinin-tagged version of DCL4 or DRB4. The results of immunoprecipitation experiments also suggest that most DCL4 is associated with DRB4, but that some DRB4 is free or associated with other proteins. Reduced accumulation of the TAS1 and TAS3 trans-acting siRNA (ta-siRNA) and over accumulation of their target mRNAs (At5g18040 and auxin response factors ARF3 and ARF4) were detected in both drb4-1 and dcl4-2 mutants. These results indicate that DRB4, together with DCL4, functions in the ta-siRNA biogenesis.
      datePublished:2007-01-14T00:00:00Z
      dateModified:2007-01-14T00:00:00Z
      pageStart:777
      pageEnd:785
      sameAs:https://doi.org/10.1007/s11103-006-9125-8
      keywords:
         DCL4
         Dicer
         DRB4
         dsRNA-binding protein
         Protein–protein interaction
         ta-siRNA
         Plant Sciences
         Biochemistry
         general
         Plant Pathology
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      name:Akihiro Hiraguri
      affiliation:
            name:Tokyo University of Agriculture and Technology
            address:
               name:Department of Applied Biological Sciences, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan
               type:PostalAddress
            type:Organization
      name:Hiromitsu Moriyama
      affiliation:
            name:Tokyo University of Agriculture and Technology
            address:
               name:Department of Applied Biological Sciences, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan
               type:PostalAddress
            type:Organization
      name:Toshiyuki Fukuhara
      affiliation:
            name:Tokyo University of Agriculture and Technology
            address:
               name:Department of Applied Biological Sciences, Tokyo University of Agriculture and Technology, Fuchu, Tokyo, Japan
               type:PostalAddress
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