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Literature summary for 2.7.7.19 extracted from

  • Nakel, K.; Bonneau, F.; Eckmann, C.R.; Conti, E.
    Structural basis for the activation of the C. elegans noncanonical cytoplasmic poly(A)-polymerase GLD-2 by GLD-3 (2015), Proc. Natl. Acad. Sci. USA, 112, 8614-8619.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
germ-line development defective GLD-2–GLD-3 complex up-regulates the expression of genes required for meiotic progression. The structure of a minimal polyadenylation complex that includes the conserved nucleotidyl-transferase core of GLD-2 and the N-terminal domain of GLD-3, to 2.3 A resolution, shows that the N-terminal domain of GLD-3 does not fold into the predicted multi-K homology domain but wraps around the catalytic domain of GLD-2. GLD-3 activates GLD-2 both indirectly by stabilizing the enzyme and directly by contributing positively charged residues near the RNA-binding cleft. Due to distinct structural features, GLD-2 displays unusual specificity in vitro for single-stranded RNAs with at least one adenosine at the 3'-end Caenorhabditis elegans

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Caenorhabditis elegans O17087
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + RNA primer isoform GLD-2 shows specificity in vitro for single-stranded RNAs with at least one adenosine at the 3'-end Caenorhabditis elegans diphosphate + RNA primer-A
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Synonyms

Synonyms Comment Organism
GLD-2
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Caenorhabditis elegans