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Literature summary for 2.7.7.48 extracted from

  • Lipardi, C.; Paterson, B.M.
    Identification of an RNA-dependent RNA polymerase in Drosophila involved in RNAi and transposon suppression (2009), Proc. Natl. Acad. Sci. USA, 106, 15645-15650.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.48

Cloned(Commentary)

Cloned (Comment) Organism
expression of FLAG-tagged D-elp1 in Spodoptera frugiperda Sf9 cells using the baculovirus transfection system, and of His-tagged wild-type and mutant enzymes in Escherichia coli. Quantitative RT-PCR analysis for the expression levels of Dcr-2 and D-elp1 RNAs in S2 cells after depletion Drosophila melanogaster

Protein Variants

Protein Variants Comment Organism
additional information construction of D-elp1 protein mutants through (1-1252 aa) and the DELTAC (1-843aa) and DELTAN (844-1252 aa) deletions. D-elp1 depletion inhibits RNAi in S2 cells but does not affect micro RNA function. D-elp1 depletion results in increased steady state levels of representative transposon RNAs and a decrease in the corresponding transposon antisense transcripts and endo siRNAs. In D-elp1 null third instar larvae transposon RNA levels are also increased and the corresponding transposon antisense RNAs are reduced Drosophila melanogaster

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
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 Drosophila melanogaster 5737
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Drosophila melanogaster D-elp1, corresponding to the largest of the three subunits in the RNA polymerase II core elongator complex, has RNA-dependent RNA polymerase activity. RdRP activity is associated with the amino terminal 96-kD fragment, DELTAC, CDS 1-2528. D-elp1 is a noncanonical RdRP that can synthesize dsRNA from different ssRNA templates using either a primer-dependent or primer-independent initiation mechanism, overview. D-elp1 associates tightly with Dcr-2 ?
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 ?

Organism

Organism UniProt Comment Textmining
Drosophila melanogaster
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-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant FLAG-tagged D-elp1 from Spodoptera frugiperda Sf9 cells by affinity chromatography. His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography Drosophila melanogaster

Source Tissue

Source Tissue Comment Organism Textmining
S2 cell
-
 Drosophila melanogaster
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information D-elp1, corresponding to the largest of the three subunits in the RNA polymerase II core elongator complex, has RNA-dependent RNA polymerase activity. RdRP activity is associated with the amino terminal 96-kD fragment, DELTAC, CDS 1-2528. D-elp1 is a noncanonical RdRP that can synthesize dsRNA from different ssRNA templates using either a primer-dependent or primer-independent initiation mechanism, overview. D-elp1 associates tightly with Dcr-2 Drosophila melanogaster ?
-
 ?

Synonyms

Synonyms Comment Organism
D-elp1
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 Drosophila melanogaster
RDRP
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 Drosophila melanogaster
RNA-dependent RNA polymerase
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 Drosophila melanogaster

General Information

General Information Comment Organism
malfunction D-elp1 depletion inhibits RNAi in S2 cells but does not affect micro RNA function. In D-elp1 null third instar larvae transposon RNA levels are also increased and the corresponding transposon antisense RNAs are reduced Drosophila melanogaster
physiological function D-elp1 is required for RNA interference, interacts with Dcr-2 protein, and has a role in transposon suppression, overview. It might be interacting with components of the RISC Drosophila melanogaster