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Literature summary for 3.1.31.1 extracted from

  • Phetrungnapha, A.; Panyim, S.; Ongvarrasopone, C.
    Penaeus monodon Tudor staphylococcal nuclease preferentially interacts with N-terminal domain of Argonaute-1 (2013), Fish Shellfish Immunol., 34, 875-884.
    View publication on PubMed
Search for more literature for 3.1.31.1

Cloned(Commentary)

Cloned (Comment) Organism
expression and interaction analysis of the enzyme fused to a GAL4-DNA-binding domain and the three Argonaute proteins in the Saccharomyces cerevisiae strain Y187 two-hybrid system, expression of N-terminally GST-tagged enzyme constructs comprising amino acid residues 1-889, 1-660, and residues 320-889, in Escherichia coli strain Rossetta (DE3) Penaeus monodon

Protein Variants

Protein Variants Comment Organism
additional information knockdown of the enzyme by dsRNA Penaeus monodon

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ calcium-dependent nuclease activity Penaeus monodon
additional information the enzyme activity is not affected by Mg2+ and Mn2+ Penaeus monodon

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
120000
-
 x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE Penaeus monodon
126000
-
 x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE Penaeus monodon

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Penaeus monodon the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA ?
-
 ?

Organism

Organism UniProt Comment Textmining
Penaeus monodon G1ARD5
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant GST-tagged enzyme constructs from Escherichia coli strain Rossetta (DE3) by glutathione affinity chromatography, and anion or cation exchange chromatography, followed by dialysis Penaeus monodon

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme possesses calcium-dependent nuclease activity specific to ssRNA, but not dsRNA and DNA Penaeus monodon ?
-
 ?
additional information substrates are double-stranded RNA targeting PAZ domain of PmAgo1, PmRab7, and gfp. The enzyme shows calcium-dependent RNase activity, overview Penaeus monodon ?
-
 ?

Subunits

Subunits Comment Organism
? x * 126000, recombinant GST-tagged enzyme, SDS-PAGE, x * 120000, recombinant GAL4-DNA-binding domain-fusion enzyme, SDS-PAGE Penaeus monodon

Synonyms

Synonyms Comment Organism
TSN
-
 Penaeus monodon
tudor staphylococcal nuclease
-
 Penaeus monodon

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Penaeus monodon

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Penaeus monodon

General Information

General Information Comment Organism
malfunction suppression of Penaeus monodon Tudor staphylococcal nuclease by double-stranded RNA results in decreasing dsRNA-mediated gene silencing activity. Knockdown of Argonaute protein PmAgo1 and the enzyme diminishes the ability of dsRNA-Rab7 to knockdown PmRab7 expression Penaeus monodon
additional information the enzyme interacts with Argonaute protein PmAgo1, but not with PmAgo2 or PmAgo3. Interaction between PmAgo and the enzyme is mediated through the N-terminal domain of PmAgo1 and the SN1-2 domains of the enzyme, interaction analysis and mapping using the two-hybrid system for different protein constructs, overview Penaeus monodon
physiological function involvement of PmAgo1 and the enzyme in shrimp RNAi pathway, RNAi-based mechanism in shrimp, overview Penaeus monodon