Literature summary for 3.1.13.4 extracted from

He, G.J.; Yan, Y.B.
Self-association of poly(A)-specific ribonuclease (PARN) triggered by the R3H domain (2014), Biochim. Biophys. Acta, 1844, 2077-2085.

Search for more literature for 3.1.13.4

Cloned(Commentary)

Cloned (Comment)	Organism
expression in HEK-293T cells	Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
74000	-	4 * 74000, calculated. Poly(A)-specific ribonuclease PARN can self-associate into tetramer and high-order oligomers both in vitro and in living cells. PARN oligomerization is triggered by the R3H domain,which leads to the solvent-exposed Trp219 fluorophore to become buried in a solvent-inaccessible microenvironment. The RRM and C-terminal domains are involved in modulating the dissociation rate of the tetrameric PARN. Tetramerization does not affect the catalytic behavior of the full-length PARN and truncated enzymes containing the RRM domain. Tetramerization significantly enhances the catalytic activity and processivity of the truncated form with the removal of the RRM and C-terminal domains	Homo sapiens
290000	-	gel filtration, full length enzyme	Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	O95453	-	-

Subunits

Subunits	Comment	Organism
tetramer	4 * 74000, calculated. Poly(A)-specific ribonuclease PARN can self-associate into tetramer and high-order oligomers both in vitro and in living cells. PARN oligomerization is triggered by the R3H domain,which leads to the solvent-exposed Trp219 fluorophore to become buried in a solvent-inaccessible microenvironment. The RRM and C-terminal domains are involved in modulating the dissociation rate of the tetrameric PARN. Tetramerization does not affect the catalytic behavior of the full-length PARN and truncated enzymes containing the RRM domain. Tetramerization significantly enhances the catalytic activity and processivity of the truncated form with the removal of the RRM and C-terminal domains	Homo sapiens

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)