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Literature summary for 3.1.13.4 extracted from

  • He, G.; Yan, Y.
    Contributions of the C-terminal domain to poly(A)-specific ribonuclease (PARN) stability and self-association (2019), Biochem. Biophys. Rep., 18, 100626 .
No PubMed abstract available
Search for more literature for 3.1.13.4

Cloned(Commentary)

Cloned (Comment) Organism
gene PARN, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21(DE3) Homo sapiens

General Stability

General Stability Organism
K+ induces additional regular secondary structures and enhances PARN stability against heat-induced inactivation, unfolding and aggregation Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
K+ K+ is essential to PARN activity and acts as an allosteric activator of PARN with multiple binding sites. K+ induces additional regular secondary structures and enhances PARN stability against heat-induced inactivation, unfolding and aggregation Homo sapiens
Mg2+ required Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens O95453
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration Homo sapiens

Subunits

Subunits Comment Organism
homodimer PARN mainly exists as a homodimer in solutions, while it can also associate into larger oligomers via its R3H domain Homo sapiens
More full-length PARN is a multi-domain protein containing the catalytic nuclease domain, the R3H domain, the RRM domain and the C-terminal intrinsically unstructured domain (CTD). Impact of CTD on PARN stability and aggregatory potency, comparing the thermal inactivation and denaturation behaviors of full-length PARN with two N-terminal fragments lacking CTD. K+ induces additional regular secondary structures and enhances PARN stability against heat-induced inactivation, unfolding and aggregation. The CTD prevents PARN from thermal inactivation but promotes thermal aggregation to initiate at a temperature much lower than that required for inactivation and unfolding. Domain architecture of PARN and effects of K+ on p74, p60 and p46 secondary and tertiary structures, overview Homo sapiens

Synonyms

Synonyms Comment Organism
PARN
-
 Homo sapiens

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
 assay at Homo sapiens

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30 50 stable at Homo sapiens
55 85 thermal denaturation of PARN in presence or absence of K+, overview Homo sapiens

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
 assay at Homo sapiens

General Information

General Information Comment Organism
additional information the C-terminal domain (CTD) prevents PARN from thermal inactivation but promotes thermal aggregation to initiate at a temperature much lower than that required for inactivation and unfolding Homo sapiens
physiological function poly(A)-specific ribonuclease (PARN) catalyzes the degradation of mRNA poly(A) tail to regulate translation efficiency and mRNA decay in higher eukaryotic cells. PARN has the unique properties of 5'-cap-binding ability, high activity, allosteric regulation, processive catalysis and highly regulated deadenylation in the cells Homo sapiens