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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.7.7.48 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

EC Number Protein Variants Comment Organism
2.7.7.48 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

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

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.48 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 ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Drosophila melanogaster
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.48 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

EC Number Source Tissue Comment Organism Textmining
2.7.7.48 S2 cell
-
Drosophila melanogaster
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 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

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

General Information

EC Number General Information Comment Organism
2.7.7.48 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
2.7.7.48 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